1mhe

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{{STRUCTURE_1mhe| PDB=1mhe | SCENE= }}
{{STRUCTURE_1mhe| PDB=1mhe | SCENE= }}
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'''THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E'''
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===THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E===
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==Overview==
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The crystal structure of the nonclassical human class lb MHC molecule HLA-E has been determined in complex with a prototypic ligand, the nonamer peptide (VMAPRTVLL), derived from the highly conserved residues 3-11 of the human MHC class la leader sequence. The mode of peptide binding retains some of the standard features observed in MHC class la complexes, but novel features imply that HLA-E has evolved to mediate specific binding to a tightly defined set of almost identical hydrophobic peptides from the highly conserved class l leader sequences. These molecular adaptations make HLA-E a rigorous checkpoint at the cell surface reporting on the integrity of the antigen processing pathway to CD94/NKG2 receptor-bearing natural killer cells.
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(as it appears on PubMed at http://www.pubmed.gov), where 9660937 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9660937}}
==About this Structure==
==About this Structure==
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[[Category: Non-classical mhc]]
[[Category: Non-classical mhc]]
[[Category: Peptide]]
[[Category: Peptide]]
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Revision as of 20:58, 2 July 2008

Image:1mhe.png

Template:STRUCTURE 1mhe

THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E

Template:ABSTRACT PUBMED 9660937

About this Structure

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

Reference

Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E., O'Callaghan CA, Tormo J, Willcox BE, Braud VM, Jakobsen BK, Stuart DI, McMichael AJ, Bell JI, Jones EY, Mol Cell. 1998 Mar;1(4):531-41. PMID:9660937

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