1hdm: Difference between revisions

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{{STRUCTURE_1hdm|  PDB=1hdm  |  SCENE=  }}  
{{STRUCTURE_1hdm|  PDB=1hdm  |  SCENE=  }}  


'''HISTOCOMPATIBILITY ANTIGEN HLA-DM'''
===HISTOCOMPATIBILITY ANTIGEN HLA-DM===




==Overview==
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The three-dimensional structure of the soluble ecto-domain of HLA-DM has been determined to 2.5 A resolution by X-ray crystallography. HLA-DM has both peptide exchange activity and acts as a chaperone to peptide-free class II MHC molecules. As predicted, the structure is similar to that of classical class II MHC molecules except that the peptide-binding site is altered to an almost fully closed groove. An unusual cavity is found at the center of the region that binds peptides in class II MHC molecules, and a tryptophanrich lateral surface is identified that is a candidate both for binding to HLA-DR, to effect catalysis, and to HLA-DO, an inhibitor.
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==About this Structure==
==About this Structure==
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[[Category: Wiley, D C.]]
[[Category: Wiley, D C.]]
[[Category: Histocompatibility protein]]
[[Category: Histocompatibility protein]]
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Revision as of 08:02, 1 July 2008

File:1hdm.png

Template:STRUCTURE 1hdm

HISTOCOMPATIBILITY ANTIGEN HLA-DMHISTOCOMPATIBILITY ANTIGEN HLA-DM

Template:ABSTRACT PUBMED 9768757

About this StructureAbout this Structure

1HDM is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation., Mosyak L, Zaller DM, Wiley DC, Immunity. 1998 Sep;9(3):377-83. PMID:9768757

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