3bev

From Proteopedia

Revision as of 17:05, 21 February 2008

11mer Structure of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding

Overview

Little is known about the structure of major histocompatibility complex (MHC) molecules outside of mammals. Only one class I molecule in the chicken MHC is highly expressed, leading to strong genetic associations with infectious pathogens. Here, we report two structures of the MHC class I molecule BF2( *)2101 from the B21 haplotype, which is known to confer resistance to Marek's disease caused by an oncogenic herpesvirus. The binding groove has an unusually large central cavity, which confers substantial conformational flexibility to the crucial residue Arg9, allowing remodeling of key peptide-binding sites. The coupled variation of anchor residues from the peptide, utilizing a charge-transfer system unprecedented in MHC molecules, allows peptides with conspicuously different sequences to be bound. This promiscuous binding extends our understanding of ways in which MHC class I molecules can present peptides to the immune system and might explain the resistance of the B21 haplotype to Marek's disease.

About this Structure

3BEV is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding., Koch M, Camp S, Collen T, Avila D, Salomonsen J, Wallny HJ, van Hateren A, Hunt L, Jacob JP, Johnston F, Marston DA, Shaw I, Dunbar PR, Cerundolo V, Jones EY, Kaufman J, Immunity. 2007 Dec;27(6):885-99. PMID:18083574

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