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Typus
Verschleierung
Bearbeiter
Graf Isolan
Gesichtet
No.png
Untersuchte Arbeit:
Seite: 15, Zeilen: 21-31
Quelle: Rudolph et al 2006
Seite(n): 432, 437, Zeilen: 432: left col. 2-9; 437: left col. 4-14
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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