1b6e
From Proteopedia
(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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caption="1b6e, resolution 2.60Å" /> | caption="1b6e, resolution 2.60Å" /> | ||
'''HUMAN CD94'''<br /> | '''HUMAN CD94'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 1B6E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1B6E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1B6E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:30:52 2008'' |
Revision as of 13:30, 15 February 2008
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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
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