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Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif.

Abstract：

:Association between the class II major histocompatibility complex (MHC) and the class II invariant chain-associated peptide (CLIP) occurs naturally as an intermediate step in the MHC class II processing pathway. Here, we report the crystal structure of the murine class II MHC molecule I-A(b) in complex with human CLIP at 2.15A resolution. The structure of I-A(b) accounts, via the peptide-binding groove's unique physicochemistry, for the distinct peptide repertoire bound by this allele. CLIP adopts a similar conformation to peptides bound by other I-A alleles, reinforcing the notion that CLIP is presented as a conventional peptide antigen. When compared to the related HLA-DR3/CLIP complex structure, the CLIP peptide displays a slightly different conformation and distinct interaction pattern with residues in I-A(b). In addition, after examining the published sequences of peptides presented by I-A(b), we discuss the possibility of predicting peptide alignment in the I-A(b) binding groove using a simple scoring matrix.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Zhu Y,Rudensky AY,Corper AL,Teyton L,Wilson IA

doi

10.1016/s0022-2836(02)01437-7

keywords:

subject

Has Abstract

pub_date

2003-02-28 00:00:00

pages

1157-74

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022283602014377

journal_volume

326

pub_type

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