1efx
From Proteopedia
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| - | [[Image:1efx.jpg|left|200px]] | + | [[Image:1efx.jpg|left|200px]] |
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| - | '''STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3''' | + | {{Structure |
| + | |PDB= 1efx |SIZE=350|CAPTION= <scene name='initialview01'>1efx</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EFX is a [ | + | 1EFX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFX OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand., Boyington JC, Motyka SA, Schuck P, Brooks AG, Sun PD, Nature. 2000 Jun 1;405(6786):537-43. PMID:[http:// | + | Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand., Boyington JC, Motyka SA, Schuck P, Brooks AG, Sun PD, Nature. 2000 Jun 1;405(6786):537-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10850706 10850706] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: receptor/mhc complex]] | [[Category: receptor/mhc complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:55:05 2008'' |
Revision as of 08:55, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3
Contents |
Overview
Target cell lysis is regulated by natural killer (NK) cell receptors that recognize class I MHC molecules. Here we report the crystal structure of the human immunoglobulin-like NK cell receptor KIR2DL2 in complex with its class I ligand HLA-Cw3 and peptide. KIR binds in a nearly orthogonal orientation across the alpha1 and alpha2 helices of Cw3 and directly contacts positions 7 and 8 of the peptide. No significant conformational changes in KIR occur on complex formation. The receptor footprint on HLA overlaps with but is distinct from that of the T-cell receptor. Charge complementarity dominates the KIR/HLA interface and mutations that disrupt interface salt bridges substantially diminish binding. Most contacts in the complex are between KIR and conserved HLA-C residues, but a hydrogen bond between Lys 44 of KIR2DL2 and Asn 80 of Cw3 confers the allotype specificity. KIR contact requires position 8 of the peptide to be a residue smaller than valine. A second KIR/HLA interface produced an ordered receptor-ligand aggregation in the crystal which may resemble receptor clustering during immune synapse formation.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
1EFX is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand., Boyington JC, Motyka SA, Schuck P, Brooks AG, Sun PD, Nature. 2000 Jun 1;405(6786):537-43. PMID:10850706
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