1NKR
INHIBITORY RECEPTOR (P58-CL42) FOR HUMAN NATURAL KILLER CELLS
Summary for 1NKR
| Entry DOI | 10.2210/pdb1nkr/pdb |
| Descriptor | P58-CL42 KIR (2 entities in total) |
| Functional Keywords | inhibitory receptor, natural killer cells, immunological receptors, immunoglobulin fold |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P43626 |
| Total number of polymer chains | 1 |
| Total formula weight | 22200.90 |
| Authors | Fan, Q.R.,Mosyak, L.,Winter, C.C.,Wagtmann, N.,Long, E.O.,Wiley, D.C. (deposition date: 1998-06-24, release date: 1998-11-11, Last modification date: 2024-10-30) |
| Primary citation | Fan, Q.R.,Mosyak, L.,Winter, C.C.,Wagtmann, N.,Long, E.O.,Wiley, D.C. Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors. Nature, 389:96-100, 1997 Cited by PubMed Abstract: Abnormal cells deficient in class I major histocompatibility complex (MHC) expression are lysed by a class of lymphocytes called natural killer (NK) cells. This lysis provides a defence against pathogens and tumour cells that downregulate MHC expression to avoid an MHC-restricted, T-cell immune response. Normal cells escape lysis because their MHC molecules are recognized by NK-cell inhibitory receptors, which inhibit lysis. Several such inhibitory receptor families have been described in humans and mice. In the human killer-cell inhibitory receptor family, individual p58 members are specific for a subset of class I human leukocyte antigen (HLA)-C molecules. The human p58 natural killer-cell inhibitory receptor clone 42 recognizes HLA-Cw4, -Cw2 and -Cw6, but not HLA-Cw3, -Cw2, -Cw7 or -Cw8, which are recognized by p58 killer-cell inhibitor receptor clone 43. We have determined the X-ray structure of the p58 NK-cell inhibitory receptor clone 42 at 1.7-A resolution. The structure has tandem immunoglobulin-like domains positioned at an acute, 60-degree angle. Loops on the outside of the elbow between the domains form a binding site projected away from the NK-cell surface. The topology of the domains and their arrangement relative to each other reveal a relationship to the haematopoietic receptor family, with implications for the signalling mechanism in NK cells. PubMed: 9288975DOI: 10.1038/38028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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