1hsa

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Template:STRUCTURE 1hsa

Contents 1 THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC 2 About this Structure 3 See Also 4 Reference

THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC

Template:ABSTRACT PUBMED 1525820

About this Structure

1hsa is a 6 chain structure of Beta-2 microglobulin and Major histocompatibility complex with sequence from Homo sapiens. The February 2005 RCSB PDB Molecule of the Month feature on Major Histocompatibility Complex by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_2. Full crystallographic information is available from OCA.

See Also

• Beta-2 microglobulin
• Major histocompatibility complex

Reference

• Madden DR, Gorga JC, Strominger JL, Wiley DC. The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC. Cell. 1992 Sep 18;70(6):1035-48. PMID:1525820
• Krebs S, Rognan D, Lopez de Castro JA. Long-range effects in protein--ligand interactions mediate peptide specificity in the human major histocompatibilty antigen HLA-B27 (B*2701). Protein Sci. 1999 Jul;8(7):1393-9. PMID:10422827 doi:10.1110/ps.8.7.1393
• Sharman GJ, Griffiths-Jones SR, Jourdan M, Searle MS. Effects of amino acid phi,psi propensities and secondary structure interactions in modulating H alpha chemical shifts in peptide and protein beta-sheet. J Am Chem Soc. 2001 Dec 12;123(49):12318-24. PMID:11734033