2PTU
Structure of NK cell receptor 2B4 (CD244)
2PTU の概要
| エントリーDOI | 10.2210/pdb2ptu/pdb |
| 分子名称 | Natural killer cell receptor 2B4 (2 entities in total) |
| 機能のキーワード | 2b4, cd244, nk cell receptor, immune system |
| 由来する生物種 | Mus musculus (house mouse) |
| 細胞内の位置 | Membrane; Single-pass type I membrane protein (Potential): Q07763 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 50107.71 |
| 構造登録者 | |
| 主引用文献 | Velikovsky, C.A.,Deng, L.,Chlewicki, L.K.,Fernandez, M.M.,Kumar, V.,Mariuzza, R.A. Structure of natural killer receptor 2B4 bound to CD48 reveals basis for heterophilic recognition in signaling lymphocyte activation molecule family. Immunity, 27:572-584, 2007 Cited by PubMed Abstract: Natural killer (NK) cells eliminate virally infected and tumor cells. Among the receptors regulating NK cell function is 2B4 (CD244), a member of the signaling lymphocyte-activation molecule (SLAM) family that binds CD48. 2B4 is the only heterophilic receptor of the SLAM family, whose other members, e.g., NK-T-B-antigen (NTB-A), are self-ligands. We determined the structure of the complex between the N-terminal domains of mouse 2B4 and CD48, as well as the structures of unbound 2B4 and CD48. The complex displayed an association mode related to, yet distinct from, that of the NTB-A dimer. Binding was accompanied by the rigidification of flexible 2B4 regions containing most of the polymorphic residues across different species and receptor isoforms. We propose a model for 2B4-CD48 interactions that permits the intermixing of SLAM receptors with major histocompatibility complex-specific receptors in the NK cell immune synapse. This analysis revealed the basis for heterophilic recognition within the SLAM family. PubMed: 17950006DOI: 10.1016/j.immuni.2007.08.019 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.38 Å) |
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