1hsa
From Proteopedia
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'''THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC''' | '''THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC''' | ||
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[[Category: Strominger, J L.]] | [[Category: Strominger, J L.]] | ||
[[Category: Wiley, D C.]] | [[Category: Wiley, D C.]] | ||
| - | [[Category: | + | [[Category: Histocompatibility antigen]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:59 2008'' | |
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Revision as of 16:11, 2 May 2008
THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC
Overview
Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 A structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a co-crystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an "anchor" side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.
About this Structure
1HSA is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 1HSA with [Major Histocompatibility Complex]. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC., Madden DR, Gorga JC, Strominger JL, Wiley DC, Cell. 1992 Sep 18;70(6):1035-48. PMID:1525820 Page seeded by OCA on Fri May 2 19:10:59 2008
