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Typus
BauernOpfer
Bearbeiter
Graf Isolan
Gesichtet
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Untersuchte Arbeit:
Seite: 13, Zeilen: 1-12
Quelle: Rudolph et al 2006
Seite(n): 420-421, 423, Zeilen: 420:right col. 37-39; 421:right col. 1-15; 423: figure 2; left col. 1-4
[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

Anmerkungen

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