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1b6e

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{{STRUCTURE_1b6e| PDB=1b6e | SCENE= }}
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'''HUMAN CD94'''
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===HUMAN CD94===
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==Overview==
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The crystal structure of the extracellular domain of CD94, a component of the CD94/NKG2 NK cell receptor, has been determined to 2.6 A resolution, revealing a unique variation of the C-type lectin fold. In this variation, the second alpha helix, corresponding to residues 102-112, is replaced by a loop, the putative carbohydrate-binding site is significantly altered, and the Ca2+-binding site appears nonfunctional. This structure may serve as a prototype for other NK cell receptors such as Ly-49, NKR-P1, and CD69. The CD94 dimer observed in the crystal has an extensive hydrophobic interface that stabilizes the loop conformation of residues 102-112. The formation of this dimer reveals a putative ligand-binding region for HLA-E and suggests how NKG2 interacts with CD94.
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(as it appears on PubMed at http://www.pubmed.gov), where 10023772 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10023772}}
==About this Structure==
==About this Structure==
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[[Category: Nkd]]
[[Category: Nkd]]
[[Category: Receptor]]
[[Category: Receptor]]
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Revision as of 15:22, 30 June 2008

Image:1b6e.png

Template:STRUCTURE 1b6e

HUMAN CD94

Template:ABSTRACT PUBMED 10023772

About this Structure

1B6E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors., Boyington JC, Riaz AN, Patamawenu A, Coligan JE, Brooks AG, Sun PD, Immunity. 1999 Jan;10(1):75-82. PMID:10023772

Page seeded by OCA on Mon Jun 30 18:22:23 2008

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