1MUJ

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

Summary for 1MUJ

• Entry DOI: 10.2210/pdb1muj/pdb
• Descriptor: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, A-B ALPHA CHAIN, H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, A BETA CHAIN, CLIP peptide, ... (5 entities in total)
• Functional Keywords: i-ab, clip, complex, antigen, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 48760.53

Authors

Zhu, Y.,Wilson, I.A. (deposition date: 2002-09-23, release date: 2003-02-18, Last modification date: 2024-10-30)

Primary citation

Zhu, Y.,Rudensky, A.Y.,Teyton, A.L.,Wilson, I.A.
Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: Prediction of an I-Ab peptide-binding motif
J.Mol.Biol., 326:1157-1174, 2003

PubMed 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.

PubMed: 12589760
DOI: 10.1016/S0022-2836(02)01437-7

Experimental method

X-RAY DIFFRACTION (2.15 Å)