1B6E

HUMAN CD94

Summary for 1B6E

• Entry DOI: 10.2210/pdb1b6e/pdb
• Descriptor: CD94 (2 entities in total)
• Functional Keywords: nk cell, receptor, c-type lectin, c-type lectin-like, nkd
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type II membrane protein: Q13241
• Total number of polymer chains: 1
• Total formula weight: 15004.53

Authors

Boyington, J.C.,Riaz, A.N.,Patamawenu, A.,Coligan, J.E.,Brooks, A.G.,Sun, P.D. (deposition date: 1999-01-14, release date: 1999-06-15, Last modification date: 2024-11-06)

Primary citation

Boyington, J.C.,Riaz, A.N.,Patamawenu, A.,Coligan, J.E.,Brooks, A.G.,Sun, P.D.
Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors.
Immunity, 10:75-82, 1999

PubMed 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.

PubMed: 10023772
DOI: 10.1016/S1074-7613(00)80008-4

Experimental method

X-RAY DIFFRACTION (2.6 Å)