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- W2069539522 abstract "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." @default.
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- W2069539522 date "1999-01-01" @default.
- W2069539522 modified "2023-10-13" @default.
- W2069539522 title "Structure of CD94 Reveals a Novel C-Type Lectin Fold" @default.
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- W2069539522 doi "https://doi.org/10.1016/s1074-7613(00)80008-4" @default.
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