2clr
From Proteopedia
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THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE
Contents |
Overview
Class I major histocompatibility complex (MHC) molecules present peptides, to CD8+ T cells for immunological surveillance (reviewed in ref. 1). The, structures of complexes of class I MHC molecules with octamer, nonamer and, decamer peptides determined until now show a common binding mode, with, both peptide termini bound in conserved pockets at the ends of the peptide, binding site. Length variations were accommodated by the peptide bulging, or zig-zagging in the middle. Here we describe the structure of a decamer, peptide which binds with the carboxy-terminal residue positioned outside, the peptide binding site. Several protein side chains have rearranged to, allow the peptide to exit. The structure suggests that even longer, peptides could bind. The energetic effect of the altered mode of binding, has been assessed by measuring the stability of the complex to thermal, denaturation. Peptides bound in this novel manner are stable at, physiological temperature, raising questions about their role in T-cell, recognition and their production by proteolytic processing.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]
About this Structure
2CLR is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a peptide extending from one end of a class I MHC binding site., Collins EJ, Garboczi DN, Wiley DC, Nature. 1994 Oct 13;371(6498):626-9. PMID:7935798
Page seeded by OCA on Mon Nov 12 21:16:58 2007
