3BEW

10mer Crystal Structure of chicken MHC class I haplotype B21

Summary for 3BEW

• Entry DOI: 10.2210/pdb3bew/pdb
• Related: 1A1M 1IM9 1KJV 1KPR 1KTL 1MHE 1OGA 1OGT 1QQD 1SYS 1YDP 2D31 2DYP 2ESV 3BEV
• Descriptor: Major histocompatibility complex class I glycoprotein haplotype B21, Beta-2-microglobulin, 10-mer from Tubulin beta-6 chain, ... (4 entities in total)
• Functional Keywords: mhc class i, chicken, 10mer, bulge, water cushion, immune response, immunoglobulin domain, mhc i, polymorphism, secreted, gtp-binding, microtubule, nucleotide-binding, immune system
• Biological source: Gallus gallus (chicken); More
• Cellular location: Secreted: P21611; Cytoplasm, cytoskeleton: P09207
• Total number of polymer chains: 6
• Total formula weight: 86624.63

Authors

Koch, M.,Camp, S.,Collen, T.,Avila, D.,Salomonsen, J.,Wallny, H.J.,van Hateren, A.,Hunt, L.,Jacob, J.P.,Johnston, F.,Marston, D.A.,Shaw, I.,Dunbar, P.R.,Cerundolo, V.,Jones, E.Y.,Kaufman, J. (deposition date: 2007-11-20, release date: 2008-01-01, Last modification date: 2024-11-13)

Primary citation

Koch, M.,Camp, S.,Collen, T.,Avila, D.,Salomonsen, J.,Wallny, H.-J.,van Hateren, A.,Hunt, L.,Jacob, J.P.,Johnston, F.,Marston, D.A.,Shaw, I.,Dunbar, P.R.,Cerundolo, V.,Jones, E.Y.,Kaufman, J.
Structures of an MHC class I molecule from b21 chickens illustrate promiscuous Peptide binding
Immunity, 27:885-899, 2007

PubMed Abstract: 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.

PubMed: 18083574
DOI: 10.1016/j.immuni.2007.11.007

Experimental method

X-RAY DIFFRACTION (2.6 Å)