1hsa: Difference between revisions
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Revision as of 00:12, 26 July 2012
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
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
