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1hsa

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[[Image:1hsa.gif|left|200px]]
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[[Image:1hsa.png|left|200px]]
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==Overview==
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{{ABSTRACT_1525820}}
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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.
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==About this Structure==
==About this Structure==
1HSA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1HSA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb62_1.html Major Histocompatibility Complex]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSA OCA].
1HSA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1HSA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb62_1.html Major Histocompatibility Complex]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSA OCA].
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==Reference==
 
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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:[http://www.ncbi.nlm.nih.gov/pubmed/1525820 1525820]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Major Histocompatibility Complex]]
[[Category: Major Histocompatibility Complex]]
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[[Category: Wiley, D C.]]
[[Category: Wiley, D C.]]
[[Category: Histocompatibility antigen]]
[[Category: Histocompatibility antigen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:30:00 2008''

Revision as of 14:30, 26 June 2008

Image:1hsa.png

Template:STRUCTURE 1hsa

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


Template:ABSTRACT 1525820

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.

Page seeded by OCA on Thu Jun 26 17:30:00 2008

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