1b6e
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of the extracellular domain of CD94, a component of | + | 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== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Boyington, J | + | [[Category: Boyington, J C.]] |
| - | [[Category: Brooks, A | + | [[Category: Brooks, A G.]] |
| - | [[Category: Coligan, J | + | [[Category: Coligan, J E.]] |
[[Category: Patamawenu, A.]] | [[Category: Patamawenu, A.]] | ||
| - | [[Category: Riaz, A | + | [[Category: Riaz, A N.]] |
| - | [[Category: Sun, P | + | [[Category: Sun, P D.]] |
[[Category: c-type lectin]] | [[Category: c-type lectin]] | ||
[[Category: c-type lectin-like]] | [[Category: c-type lectin-like]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:59 2008'' |
Revision as of 09:52, 21 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
Page seeded by OCA on Thu Feb 21 11:51:59 2008
