1b6e
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(New page: 200px<br /> <applet load="1b6e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b6e, resolution 2.60Å" /> '''HUMAN CD94'''<br />...)
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Revision as of 14:00, 12 November 2007
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HUMAN CD94
Overview
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.
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 Nov 12 16:06:34 2007
