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Typus
Verschleierung
Bearbeiter
Graf Isolan
Gesichtet
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Untersuchte Arbeit:
Seite: 12, Zeilen: 27-31
Quelle: Rudolph et al 2006
Seite(n): 421, Zeilen: 421:left col. 7-15 - right col. 1-5
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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