Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors
| Autor: | J C, Boyington, A N, Riaz, A, Patamawenu, J E, Coligan, A G, Brooks, P D, Sun |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Protein Folding Binding Sites Membrane Glycoproteins Sequence Homology Amino Acid Histocompatibility Antigens Class I Molecular Sequence Data Crystallography X-Ray Killer Cells Natural Antigens CD HLA Antigens Lectins Receptors Mitogen Humans Receptors Natural Killer Cell Lectins C-Type Amino Acid Sequence Receptors Immunologic NK Cell Lectin-Like Receptor Subfamily C Dimerization NK Cell Lectin-Like Receptor Subfamily D |
| Zdroj: | Immunity. 10(1) |
| ISSN: | 1074-7613 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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