1efx

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[[Image:1efx.jpg|left|200px]]
[[Image:1efx.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_1efx| PDB=1efx | SCENE= }}
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|RELATEDENTRY=[[2dl2|2dl2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efx OCA], [http://www.ebi.ac.uk/pdbsum/1efx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1efx RCSB]</span>
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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 OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3'''
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[[Category: Schuck, P.]]
[[Category: Schuck, P.]]
[[Category: Sun, P D.]]
[[Category: Sun, P D.]]
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[[Category: class i]]
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[[Category: Class i]]
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[[Category: hla]]
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[[Category: Hla]]
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[[Category: immunoglobulin fold]]
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[[Category: Immunoglobulin fold]]
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[[Category: kir]]
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[[Category: Kir]]
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[[Category: mhc]]
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[[Category: Mhc]]
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[[Category: nk cell receptor]]
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[[Category: Nk cell receptor]]
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[[Category: receptor/mhc complex]]
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[[Category: Receptor/mhc complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:02:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:44 2008''
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Revision as of 12:02, 2 May 2008

Template:STRUCTURE 1efx

STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3


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.

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 Page seeded by OCA on Fri May 2 15:02:56 2008

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