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spinqualitylabelsall models 1muj, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of murine class II MHC I-Ab in complex with a human CLIP peptide

Overview

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.

About this Structure

1MUJ is a Protein complex structure of sequences from Homo sapiens and Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif., Zhu Y, Rudensky AY, Corper AL, Teyton L, Wilson IA, J Mol Biol. 2003 Feb 28;326(4):1157-74. PMID:12589760

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