Structural basis of MHC class I recognition by natural killer cell receptors
| Autor: | M W, Sawicki, N, Dimasi, K, Natarajan, J, Wang, D H, Margulies, R A, Mariuzza |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Macromolecular Substances Molecular Sequence Data HLA-C Antigens Ligands Mice Leukocyte Immunoglobulin-like Receptor B1 Receptors KIR Antigens CD Animals Antigens Ly Humans Lectins C-Type Amino Acid Sequence Receptors Immunologic Histocompatibility Antigen H-2D Binding Sites Molecular Structure Sequence Homology Amino Acid Histocompatibility Antigens Class I H-2 Antigens Membrane Proteins Killer Cells Natural Receptors KIR2DL2 Carrier Proteins NK Cell Lectin-Like Receptor Subfamily A Receptors NK Cell Lectin-Like |
| Zdroj: | Immunological reviews. 181 |
| ISSN: | 0105-2896 |
| Popis: | Natural killer (NK)-cell function is regulated by NK receptors that recognize MHC class I (MHC-I) molecules on target cells. Two structurally distinct families of NK receptors have been identified, the immunoglobulin-like family (killer cell immunoglobulin-like receptors (KIRs), leukocyte immunoglobulin-like receptors (LIRs)) and the C-type lectin-like family (Ly49, CD94/NKG2A, NKG2D, CD69). Recently, the three-dimensional structures of several NK receptors were determined, in free form or bound to MHC-I. These include those of unbound KIRs, NKG2D, CD69, LIR-1 and the CD94 subunit of the CD94/NKG2A heterodimer. Together, these structures define the basic molecular architecture of both the immunoglobulin-like and C-type lectin-like families of NK receptors. In addition, crystal structures have been reported for the complex between Ly49A and H-2Dd, and for KIR2DL2 bound to HLA-Cw3. The complex structures provide a framework for understanding MHC-I recognition by NK receptors from both families and reveal striking differences in the nature of this recognition, despite the receptors' functional similarity. |
| Databáze: | OpenAIRE |
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