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| Autor | Markus G. Rudolph, Robyn L. Stanfield, and Ian A.Wilson |
| Titel | How TCRs Bind MHCs, Peptides, and Coreceptors |
| Zeitschrift | Annual Review of Immunology |
| Datum | 16. January 2006 |
| Nummer | 24 |
| Seiten | 419-466 |
| Anmerkung | Volume publication date April 2006; first published online as a Review in Advance on January 16, 2006 |
| DOI | 10.1146/annurev.immunol.23.021704.115658 |
| URL | http://www.annualreviews.org/doi/abs/10.1146/annurev.immunol.23.021704.115658 |
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| Fußnoten | ja |
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| Both classes of MHC molecules are heterodimers with similar architectures and are composed of three domains, one α-helix/β-sheet superdomain that forms the peptide-binding site and two immunoglobulin (Ig)-like domains (Fig.1) (Bjorkman et al., 1987b; Brown et al., 1993; Fremont et al., 1996; Madden et al., 1993; Matsumura et al., 1992; Stern and Wiley, 1994). The overall architecture is the same in both MHC classes, where a seven-[stranded β-sheet represents the floor of the peptide-binding groove, and the sides are formed by two long α-helices, that straddle the β-sheet.]
Bjorkman, P.J., Saper, M.A., Samraoui, B., Bennett, W.S., Strominger, J.L., and Wiley, D.C. (1987b). Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329, 506-512. Brown, J.H., Jardetzky, T.S., Gorga, J.C., Stern, L.J., Urban, R.G., Strominger, J.L., and Wiley, D.C. (1993). Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 364, 33-39. Fremont, D.H., Hendrickson, W.A., Marrack, P., and Kappler, J. (1996). Structures of an MHC class II molecule with covalently bound single peptides. Science 272, 1001-1004. Madden, D.R., Garboczi, D.N., and Wiley, D.C. (1993). The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75, 693-708. Matsumura, M., Fremont, D.H., Peterson, P.A., and Wilson, I.A. (1992). Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257, 927-934. Stern, L.J., and Wiley, D.C. (1994). Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2, 245-251. |
Both classes of MHC are heterodimers with similar architectures and are composed of three domains, one α-helix/β-sheet (αβ) superdomain that forms the peptide-binding site and two Ig-like domains. [...] Notwithstanding, in both MHC classes, the overall architecture is the same where a seven-stranded β-sheet represents the floor of the binding groove, and the sides are formed by two long α-helices (or continuous α-helical segments in the α2- or β1-helices) that straddle the [β-sheet (Figure 2a,b).]
43. Madden DR, Garboczi DN, Wiley DC. 1993. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLAA2. Cell 75:693–708 44. Stern LJ,Wiley DC. 1994. Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2:245–51 |
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| [The overall architecture is the same in both MHC classes, where a seven-]stranded β-sheet represents the floor of the peptide-binding groove, and the sides are formed by two long α-helices, that straddle the β-sheet.
In MHC class I molecules, the peptide-binding site is constructed from the heavy chain only, and an additional 12-kDa light chain subunit, β2-microglobulin (β2m), associates with the α3 domain of the heavy chain (Fig.1). |
[Page 420]
In class I MHC molecules, the peptide-binding site (called the α1α2 domain) is constructed from the heavy chain only, and an additional light chain subunit, β2-microglobulin (β2m), associates with α3 of the heavy chain. In contrast, the class II MHC peptide-binding site is assembled from two heavy chains (α1β1). Notwithstanding, in both MHC classes, the overall architecture is the same where a seven-stranded β-sheet represents the floor of the binding groove, and the sides are formed by two long α-helices (or continuous α-helical segments in the α2- or β1-helices) that straddle the [Page 421] β-sheet (Figure 2a,b). |
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| [3.] Analyse:Asa/Fragment 012 27 - Diskussion Zuletzt bearbeitet: 2014-10-09 00:13:06 Graf Isolan | Asa, Fragment, Rudolph et al 2006, SMWFragment, Schutzlevel, Verschleierung, ZuSichten |
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| The groove is generally long enough to accommodate 8 or 9 residues in an extended conformation (Madden et al., 1991) with the termini and the so-called anchor residues buried in specificity pockets that differ from allele to allele (Fremont et al., 1992; Madden et al., 1993). This binding mode leaves the upward-pointing peptide side chains available for direct interaction with the TcR. Longer peptides can either [bind by extension at the C terminus (Stern et al., 1994) or due to the fixing of their termini, bulge out of the binding groove, providing additional surface area for TcR recognition (Speir et al., 2001; Tynan et al., 2005).]
Fremont, D.H., Matsumura, M., Stura, E.A., Peterson, P.A., and Wilson, I.A. (1992). Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science 257, 919-927. Madden, D.R., Gorga, J.C., Strominger, J.L., and Wiley, D.C. (1991). The structure of HLAB27 reveals nonamer self-peptides bound in an extended conformation. Nature 353, 321-325. Madden, D.R., Garboczi, D.N., and Wiley, D.C. (1993). The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75, 693-708. Speir, J.A., Stevens, J., Joly, E., Butcher, G.W., and Wilson, I.A. (2001). Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa. Immunity 14, 81-92. Stern, L.J., and Wiley, D.C. (1994). Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2, 245-251. Tynan, F.E., Burrows, S.R., Buckle, A.M., Clements, C.S., Borg, N.A., Miles, J.J., Beddoe, T., Whisstock, J.C., Wilce, M.C., Silins, S.L., et al. (2005). T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide. Nat Immunol 6, 1114-1122. |
Class I MHC molecules usually bind peptides of 8–10 residues length (on average 9-mers, P1–P9) (Figure 3) in an extended conformation with the termini and the so-called anchor residues buried in specificity pockets that differ from allele to allele (42, 43). This binding mode leaves the upward-pointing peptide side chains available for direct interaction with the TCR (Figure 3). Longer peptides can either bind by extension at the C terminus (44) or, due to the fixing of their termini, bulge out of the binding groove, providing additional surface area for TCR recognition (22, 45).
22. Tynan FE, Borg NA, Miles JJ, Beddoe T, El-Hassen D, et al. 2005. High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance. J. Biol. Chem. 280:23900–9 42. Fremont DH, Matsumura M, Stura EA, Peterson PA, Wilson IA. 1992. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science 257:919–27 43. Madden DR, Garboczi DN, Wiley DC. 1993. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLAA2. Cell 75:693–708 44. Stern LJ, Wiley DC. 1994. Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2:245–51 45. Speir JA, Stevens J, Joly E, Butcher GW, Wilson IA. 2001. Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa. Immunity 14:81–92 |
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| [Longer peptides can either] bind by extension at the C terminus (Stern et al., 1994) or due to the fixing of their termini, bulge out of the binding groove, providing additional surface area for TcR recognition (Speir et al., 2001; Tynan et al., 2005).
[Figure 1: Architecture of MHC-like molecules (a) Class I molecules consist of a heavy chain (blue) and a light β2m chain (orange). The peptide-binding site is formed exclusively by elements of the heavy chain (b) Class II molecules; the peptide-binding site is assembled of both subunits. (Rudolph et. al. 2006) [...] ] In contrast, the MHC class II molecule are assembled from two heavy chains (αβ) in which the peptide-binding groove is open at either end, and the peptide termini are not fixed so that bound peptides are usually significantly longer than in MHC class I (Fig.1). The MHC class II allows presentation of peptides of 13-18 residues. The peptide backbone in MHC class II is confined mainly to a poly-proline type II conformation (Stern et al., 1994) and resides slightly deeper in the binding groove. Thus, the bound peptide is more accessible for TcR inspection in MHC class I due to its ability to bulge out of the groove, even for 9-mer peptides, however, in MHC class II the termini particularly the N-terminal extension, can play a major role in the TcR interaction. Speir, J.A., Stevens, J., Joly, E., Butcher, G.W., and Wilson, I.A. (2001). Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa. Immunity 14, 81-92. Rudolph, M.G., Stanfield, R.L., and Wilson, I.A. (2006). How TCRs bind MHCs, peptides, and coreceptors. Annu Rev Immunol 24, 419-466. Stern, L.J., and Wiley, D.C. (1994). Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2, 245-251. Tynan, F.E., Burrows, S.R., Buckle, A.M., Clements, C.S., Borg, N.A., Miles, J.J., Beddoe, T., Whisstock, J.C., Wilce, M.C., Silins, S.L., et al. (2005). T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide. Nat Immunol 6, 1114-1122. |
[Page 420]
In contrast, the class II MHC peptide-binding site is assembled from two heavy chains (α1β1). [Page 421] Longer peptides can either bind by extension at the C terminus (44) or, due to the fixing of their termini, bulge out of the binding groove, providing additional surface area for TCR recognition (22, 45). In class II MHC, the groove is open at either end, and the peptide termini are not fixed so that bound peptides are usually significantly longer than in MHC class I (Figure 3). The peptide backbone in class II MHC is confined mainly to a poly-proline type II conformation (44) and resides slightly deeper in the binding groove. Thus, the bound peptide (P1–P9) is more accessible for TCR inspection in MHC class I due to its ability to bulge out of the groove, even for [Page 423] [Figure 2 Architecture of MHC-like molecules. The top panel shows the domain organization of the MHC(-like) molecules and the lower panel focuses on the ligand and/or receptor binding sites. (a) Class I molecules consist of a heavy chain (blue) and a light β2m chain (orange). The peptide-binding site is formed exclusively by elements of the heavy chain, whereas in class II molecules (b), it is assembled from both subunits. ] 9-mer peptides; however, in MHC class II, the termini, particularly the N-terminal extension (P-4 to P-1), can play a major role in the TCR interaction. 22. Tynan FE, Borg NA, Miles JJ, Beddoe T, El-Hassen D, et al. 2005. High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance. J. Biol. Chem. 280:23900–9 44. Stern LJ, Wiley DC. 1994. Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2:245–51 45. Speir JA, Stevens J, Joly E, Butcher GW, Wilson IA. 2001. Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa. Immunity 14:81–92 |
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| 1.1.1.2 The T cell receptor
TcRs are cell surface heterodimers consisting of either disulfide-linked α and β or γ and δ -chains (Brenner et al., 1986; Chien et al., 1987; Hedrick et al., 1984; Koning et al., 1987; Saito et al., 1984; Winoto and Baltimore, 1989; Yanagi et al., 1984). Sequence analyses correctly predicted that TcRs would share a domain organization and binding mode similar to those of antibody Fab fragments (Davis and Bjorkman, 1988). Brenner, M.B., McLean, J., Dialynas, D.P., Strominger, J.L., Smith, J.A., Owen, F.L., Seidman, J.G., Ip, S., Rosen, F., and Krangel, M.S. (1986). Identification of a putative second T-cell receptor. Nature 322, 145-149. Chien, Y.H., Iwashima, M., Wettstein, D.A., Kaplan, K.B., Elliott, J.F., Born, W., and Davis, M.M. (1987). T-cell receptor delta gene rearrangements in early thymocytes. Nature 330, 722-727. Davis, M.M., and Bjorkman, P.J. (1988). T-cell antigen receptor genes and T-cell recognition. Nature 334, 395-402. Hedrick, S.M., Cohen, D.I., Nielsen, E.A., and Davis, M.M. (1984). Isolation of cDNA clones encoding T cell-specific membrane-associated proteins. Nature 308, 149-153. Koning, F., Stingl, G., Yokoyama, W.M., Yamada, H., Maloy, W.L., Tschachler, E., Shevach, E.M., and Coligan, J.E. (1987). Identification of a T3-associated gamma delta T cell receptor on Thy-1+ dendritic epidermal Cell lines. Science 236, 834-837. Saito, H., Kranz, D.M., Takagaki, Y., Hayday, A.C., Eisen, H.N., and Tonegawa, S. (1984). A third rearranged and expressed gene in a clone of cytotoxic T lymphocytes. Nature 312, 36-40. Winoto, A., and Baltimore, D. (1989). Separate lineages of T cells expressing the alpha beta and gamma delta receptors. Nature 338, 430-432. Yanagi, Y., Yoshikai, Y., Leggett, K., Clark, S.P., Aleksander, I., and Mak, T.W. (1984). A human T cell-specific cDNA clone encodes a protein having extensive homology to immunoglobulin chains. Nature 308, 145-149. |
αβ and γδ TCRs
TCRs are cell surface heterodimers consisting of either disulfide-linked α- and β- or γ- and δ-chains. Sequence analyses correctly predicted that TCRs would share a domain organization and binding mode similar to those of antibody Fab fragments (69, 70). 69. Claverie JM, Prochnicka-Chalufour A, Bougueleret L. 1989. Implications of a Fab-like structure for the T-cell receptor. Immunol. Today 10:10–14 70. Davis MM, Bjorkman PJ. 1988. T-cell antigen receptor genes and T-cell recognition. Nature 334:395–402 |
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| The first crystal structures of TcRs with MHC class I molecules led to proposals that the TcR orientation is approximately diagonal with a mean around 35° (Rudolph and Wilson, 2002). By contrast, in the first MHC class II complexes, the orientation was described as being closer to 90° (Hennecke et al., 2000; Reinherz et al., 1999) suggesting a different binding mode between the MHC classes (Wang and Reinherz, 2002).
Insight into the structural changes that supplement TcR-pMHC engagement must include crystal structures of the same TcR in its free and bound forms or of the same TcR bound to different pMHCs. Until recently, only two well-studied systems, the 2C and A6 TcRs, fullfilled these requirements. The 2C system allowed comparison of the free 2C TcR (Garcia et al., 1996a) with an agonist (Garcia et al., 1998) and a superagonist peptide (Degano et al., 2000) in complex with the same H-2Kb MHC. Degano, M., Garcia, K.C., Apostolopoulos, V., Rudolph, M.G., Teyton, L., and Wilson, I.A. (2000). A functional hot spot for antigen recognition in a superagonist TCR/MHC complex. Immunity 12, 251-261. Garcia, K.C., Degano, M., Pease, L.R., Huang, M., Peterson, P.A., Teyton, L., and Wilson, I.A. (1998). Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279, 1166-1172. Garcia, K.C., Degano, M., Stanfield, R.L., Brunmark, A., Jackson, M.R., Peterson, P.A., Teyton, L., and Wilson, I.A. (1996a). An alphabeta T cell receptor structure at 2.5 A and its orientation in the TCR-MHC complex. Science 274, 209-219. Hennecke, J., Carfi, A., and Wiley, D.C. (2000). Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLADR1. EMBO J 19, 5611-5624. Reinherz, E.L., Tan, K., Tang, L., Kern, P., Liu, J., Xiong, Y., Hussey, R.E., Smolyar, A., Hare, B., Zhang, R., et al. (1999). The crystal structure of a T cell receptor in complex with peptide and MHC class II. Science 286, 1913-1921. Rudolph, M.G., and Wilson, I.A. (2002). The specificity of TCR/pMHC interaction. Curr Opin Immunol 14, 52-65. Wang, J.H., and Reinherz, E.L. (2002). Structural basis of T cell recognition of peptides bound to MHC molecules. Mol Immunol 38, 1039-1049. |
[Seite 432]
The first crystal structures of TCRs with class I molecules led to proposals that the TCR orientation is approximately diagonal with a mean around 35◦ (36). By contrast, in the first class II complexes, the orientation was described as being closer to perpendicular (15, 18), suggesting a different binding mode between the MHC classes (81). [Seite 437] Insight into the structural changes that accompany TCR/antigen engagement (i.e., induced fit) must include crystal structures of the same TCR in its free and bound forms or of the same TCR bound to different pMHCs. Until recently, only two well-studied systems, the 2C and A6 TCRs, fulfilled these requirements. The 2C system allowed comparison of the free 2C TCR (7) with an agonist (12) and a superagonist peptide (17) in complex with the same H-2Kb MHC (Figure 7a). 7. Garcia KC, Degano M, Stanfield RL, Brunmark A, Jackson MR, et al. 1996. An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex. Science 274:209–19 12. Garcia KC, Degano M, Pease LR, Huang M, Peterson PA, et al. 1998. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279:1166–72 15. Reinherz EL, Tan K, Tang L, Kern P, Liu J, et al. 1999. The crystal structure of a T cell receptor in complex with peptide and MHC class II. Science 286:1913–21 17. Degano M, Garcia KC, Apostolopoulos V, Rudolph MG, Teyton L, Wilson IA. 2000. A functional hot spot for antigen recognition in a superagonist TCR/MHC complex. Immunity 12:251–61 18. Hennecke J, Carfi A, Wiley DC. 2000. Structure of a covalently stabilized complex of a human αβT-cell receptor, influenzaHApeptide andMHCclass II molecule, HLA-DR1. EMBO J. 19:5611–24 36. Rudolph MG,Wilson IA. 2002. The specificity of TCR/pMHC interaction. Curr. Opin. Immunol. 14:52–65 81. Wang JH, Reinherz EL. 2002. Structural basis of T cell recognition of peptides bound to MHC molecules. Mol. Immunol. 38:1039–49 |
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| [This comparison disclosed a] functional hotspot between the CDR3 loops in the 2C TcR that finely discriminated between side chains and conformations of centrally located peptide residues through increased complementarity and additional hydrogen bonds. In the A6 system, altered peptide ligands (APLs) induced only subtle conformational changes in the TcR. In both the 2C and A6 systems, conformational changes are restricted mainly to the CDR3 loop regions, and the largest conformational differences were observed when comparing free versus bound TcRs (Rudolph and Wilson, 2002).
Rudolph, M.G., and Wilson, I.A. (2002). The specificity of TCR/pMHC interaction. Curr Opin Immunol 14, 52-65. |
This comparison disclosed a functional hotspot between the CDR3 loops in the 2C TCR that finely discriminated between side chains and conformations of centrally located peptide residues through increased complementarity and additional hydrogen bonds. In the A6 system (13, 14), altered peptide ligands (APLs), i.e., peptides of slightly different sequence than the natural ligand, induced only subtle conformational changes in the TCR (Figure 7b). In both the 2C and A6 systems, conformational changes are restricted mainly to the CDR3 loop regions, and the largest conformational differences were observed when comparing free versus bound TCR (36).
13. Ding YH, Smith KJ, Garboczi DN, Utz U, Biddison WE,Wiley DC. 1998. Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity 8:403–11 14. Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC. 1999. Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity 11:45–56 36. Rudolph MG,Wilson IA. 2002. The specificity of TCR/pMHC interaction. Curr. Opin. Immunol. 14:52–65 |
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| Compared with αβ TcRs, much less is known about γδ TcRs (Fig.2). The biological function of the γδ TcRs is also ill defined. γδ T cells appear to respond to bacterial and parasitic infections (Morita et al., 1995) and primarily recognize phosphate-containing antigens (phosphoantigens) from mycobacteria by an unknown mechanism (Belmant et al., 1999; Morita et al., 1995).
Belmant, C., Espinosa, E., Poupot, R., Peyrat, M.A., Guiraud, M., Poquet, Y., Bonneville, M., and Fournie, J.J. (1999). 3-Formyl-1-butyl pyrophosphate A novel mycobacterial metabolite-activating human gammadelta T cells. J Biol Chem 274, 32079-32084. Morita, C.T., Beckman, E.M., Bukowski, J.F., Tanaka, Y., Band, H., Bloom, B.R., Golan, D.E., and Brenner, M.B. (1995). Direct presentation of nonpeptide prenyl pyrophosphate antigens to human gamma delta T cells. Immunity 3, 495-507. |
Compared with αβ TCRs, where a variety of structures have been determined since 1996, much less is known about γδ TCRs. [...] γδ T cells appear to respond to bacterial and parasitic infections (72) and primarily recognize phosphate-containing antigens (phosphoantigens) from mycobacteria by an unknown mechanism (72, 73).
72. Morita CT, Beckman EM, Bukowski JF, Tanaka Y, Band H, et al. 1995. Direct presentation of nonpeptide prenyl pyrophosphate antigens to human γδ T cells. Immunity 3:495–507 73. Belmant C, Espinosa E, Poupot R, Peyrat MA, Guiraud M, et al. 1999. 3-Formyl-1-butyl pyrophosphate, a novel mycobacterial metabolite activating human γδ T cells. J. Biol. Chem. 274:32079–84 |
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