1hoc: Difference between revisions

Revision as of 08:28, 1 July 2008

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File:1hoc.png

Template:STRUCTURE 1hoc

THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTIONTHE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION

Template:ABSTRACT PUBMED 7506996

About this StructureAbout this Structure

1HOC is a Protein complex structure of sequences from Influenza a virus and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection., Young AC, Zhang W, Sacchettini JC, Nathenson SG, Cell. 1994 Jan 14;76(1):39-50. PMID:7506996

Page seeded by OCA on Tue Jul 1 08:28:03 2008

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OCA

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-'''THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION'''
+===THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION===
-==Overview==
+<!--
-Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.
+The line below this paragraph, {{ABSTRACT_PUBMED_7506996}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_7506996}}
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 [[Category: Zhang, W.]]
 [[Category: Histocompatibility antigen]]
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