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From Proteopedia
Revision as of 12:53, 28 September 2014 by OCA (Talk | contribs)
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Young AC, Zhang W, Sacchettini JC, Nathenson SG. The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection. Cell. 1994 Jan 14;76(1):39-50. PMID:7506996
