1mhe: Difference between revisions

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|PDB= 1mhe |SIZE=350|CAPTION= <scene name='initialview01'>1mhe</scene>, resolution 2.85&Aring;
|PDB= 1mhe |SIZE=350|CAPTION= <scene name='initialview01'>1mhe</scene>, resolution 2.85&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE= HLA-E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BETA-2-MICROGLOBULIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= HLA-E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BETA-2-MICROGLOBULIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhe OCA], [http://www.ebi.ac.uk/pdbsum/1mhe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mhe RCSB]</span>
}}
}}


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==Overview==
==Overview==
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.
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.
==Disease==
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]]


==About this Structure==
==About this Structure==
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[[Category: Tormo, J.]]
[[Category: Tormo, J.]]
[[Category: Willcox, B E.]]
[[Category: Willcox, B E.]]
[[Category: SO4]]
[[Category: beta 2 microglobulin]]
[[Category: beta 2 microglobulin]]
[[Category: class ib mhc]]
[[Category: class ib mhc]]
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[[Category: peptide]]
[[Category: peptide]]


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