2OR7
Tim-2
2OR7 の概要
| エントリーDOI | 10.2210/pdb2or7/pdb |
| 関連するPDBエントリー | 2OR8 |
| 分子名称 | T-cell immunoglobulin and mucin domain-containing protein 2, ACETATE ION (3 entities in total) |
| 機能のキーワード | beta barrel, immunoglobulin fold, igv domain, tim, immune system |
| 由来する生物種 | Mus musculus (house mouse) |
| 細胞内の位置 | Cell membrane; Single-pass type I membrane protein: Q8R183 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 25442.12 |
| 構造登録者 | Santiago, C.,Ballesteros, A.,Kaplan, G.G.,Casasnovas, J.M. (登録日: 2007-02-02, 公開日: 2007-04-03, 最終更新日: 2024-11-06) |
| 主引用文献 | Santiago, C.,Ballesteros, A.,Tami, C.,Martinez-Munoz, L.,Kaplan, G.G.,Casasnovas, J.M. Structures of T Cell Immunoglobulin Mucin Receptors 1 and 2 Reveal Mechanisms for Regulation of Immune Responses by the TIM Receptor Family. Immunity, 26:299-310, 2007 Cited by PubMed Abstract: The T cell immunoglobulin mucin (TIM) receptors are involved in the regulation of immune responses, autoimmunity, and allergy. Structures of the N-terminal ligand binding domain of the murine mTIM-1 and mTIM-2 receptors revealed an immunoglobulin (Ig) fold, with four Cys residues bridging a distinctive CC' loop to the GFC beta-sheet. The structures showed two ligand-recognition modes in the TIM family. The mTIM-1 structure identified a homophilic TIM-TIM adhesion interaction, whereas the mTIM-2 domain formed a dimer that prevented homophilic binding. Biochemical, mutational, and cell adhesion analyses confirmed the divergent ligand-binding modes revealed by the structures. Structural features characteristic of mTIM-1 appear conserved in human TIM-1, which also mediated homophilic interactions. The extracellular mucin domain enhanced binding through the Ig domain, modulating TIM receptor functions. These results explain the divergent immune functions described for the murine receptors and the role of TIM-1 as a cell adhesion receptor in renal regeneration and cancer. PubMed: 17363299DOI: 10.1016/j.immuni.2007.01.014 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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