1b6e: Difference between revisions
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'''HUMAN CD94''' | '''HUMAN CD94''' | ||
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[[Category: Riaz, A N.]] | [[Category: Riaz, A N.]] | ||
[[Category: Sun, P D.]] | [[Category: Sun, P D.]] | ||
[[Category: | [[Category: C-type lectin]] | ||
[[Category: | [[Category: C-type lectin-like]] | ||
[[Category: | [[Category: Nk cell]] | ||
[[Category: | [[Category: Nkd]] | ||
[[Category: | [[Category: Receptor]] | ||
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Revision as of 08:07, 2 May 2008
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 Fri May 2 11:07:45 2008
