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'''STRUCTURE OF THE HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN, HLA-A2''' | '''STRUCTURE OF THE HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN, HLA-A2''' | ||
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[[Category: Strominger, J L.]] | [[Category: Strominger, J L.]] | ||
[[Category: Wiley, D C.]] | [[Category: Wiley, D C.]] | ||
[[Category: | [[Category: Histocompatibility antigen]] | ||
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Revision as of 18:58, 2 May 2008
STRUCTURE OF THE HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN, HLA-A2
OverviewOverview
The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel beta-strands topped by alpha-helices. A large groove between the alpha-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2.
About this StructureAbout this Structure
1HLA is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the human class I histocompatibility antigen, HLA-A2., Bjorkman PJ, Saper MA, Samraoui B, Bennett WS, Strominger JL, Wiley DC, Nature. 1987 Oct 8-14;329(6139):506-12. PMID:3309677 Page seeded by OCA on Fri May 2 18:58:35 2008