Structure of killer cell immunoglobulin-like receptors and their recognition of the class I MHC molecules
| Autor: | J C, Boyington, A G, Brooks, P D, Sun |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Binding Sites Molecular Structure Sequence Homology Amino Acid Macromolecular Substances Histocompatibility Antigens Class I Molecular Sequence Data Membrane Proteins Hydrogen Bonding HLA-C Antigens Ligands Mice Receptors KIR Receptors KIR2DL2 Animals Antigens Ly Humans Lectins C-Type Amino Acid Sequence Receptors Immunologic Carrier Proteins Receptors NK Cell Lectin-Like |
| Zdroj: | Immunological reviews. 181 |
| ISSN: | 0105-2896 |
| Popis: | The recognition of class I MHC molecules by killer cell immunoglobulin-like receptors (KIR) constitutes an integral part of immune surveillance by the innate immune system. To understand the molecular basis of this recognition, the structures of several members of this superfamily have been determined. Despite their functional diversity, members of this superfamily share many conserved structural features. A central question is how these receptors recognize their ligands. The recent determination of the crystal structure of KIR2DL2 in complex with HLA-Cw3 has revealed the molecular mechanisms underpinning this interaction, which ultimately modulates the cytolytic activity of natural killer cells. While the recognition of MHC molecules by KIR is characterized by a number of unique features, some unexpected similarities with T-cell receptor recognition of MHC molecules are also observed. The detailed interactions between KIR2DL2 and HLA-Cw3 and their functional implications will be reviewed here. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text