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Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins by Ora Schueler‐Furman; Yael Altuvia; Hanah Margalit is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins about?

Antigenic peptides bind to major histocompatibility complex (MHC) molecules as a prerequisite for their presentation to T cells. In this study, we investigate possible structural preferences of MHC-binding peptides by examining the conformation space defined by the structures of these peptides within their native source proteins. Comparison of the conformation space of the native structures of MHC-binding nonamers and a corresponding conformation space defined by a random set of nonamers showed no significant difference. This suggests that the environment of the MHC binding groove has evolved to bind peptides with essentially any "structural background." A slight tendency for an extended beta-conformation at positions 8 and 9 was observed for the set of native structures. We suggest that such a preference may facilitate the binding of the C-terminal anchor position of processed peptides into the corresponding specificity pocket. MHC-binding peptides represent examples of short subsequences that are present in two different structural environments: within their native protein and within the MHC binding groove. Comparison of the native and of the bound structure of the peptides showe

Who reads Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins?

Author

Ora Schueler‐Furman; Yael Altuvia; Hanah Margalit

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)