2LZL
FGFR3tm
2LZL の概要
| エントリーDOI | 10.2210/pdb2lzl/pdb |
| NMR情報 | BMRB: 18763 |
| 分子名称 | Fibroblast growth factor receptor 3 (1 entity in total) |
| 機能のキーワード | transmembrane domain, fibroblast growth factor receptor, dimerization, tyrosine kinase, membrane protein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein (By similarity). Isoform 3: Secreted. Isoform 4: Cell membrane; Single-pass type I membrane protein (By similarity): P22607 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 9208.65 |
| 構造登録者 | Lesovoy, D.M.,Bocharov, E.V.,Goncharuk, S.A.,Arseniev, A.S. (登録日: 2012-10-04, 公開日: 2013-10-09, 最終更新日: 2024-05-01) |
| 主引用文献 | Bocharov, E.V.,Lesovoy, D.M.,Goncharuk, S.A.,Goncharuk, M.V.,Hristova, K.,Arseniev, A.S. Structure of FGFR3 Transmembrane Domain Dimer: Implications for Signaling and Human Pathologies. Structure, 21:2087-2093, 2013 Cited by PubMed Abstract: Fibroblast growth factor receptor 3 (FGFR3) transduces biochemical signals via lateral dimerization in the plasma membrane, and plays an important role in human development and disease. Eight different pathogenic mutations, implicated in cancers and growth disorders, have been identified in the FGFR3 transmembrane segment. Here, we describe the dimerization of the FGFR3 transmembrane domain in membrane-mimicking DPC/SDS (9/1) micelles. In the solved NMR structure, the two transmembrane helices pack into a symmetric left-handed dimer, with intermolecular stacking interactions occurring in the dimer central region. Some pathogenic mutations fall within the helix-helix interface, whereas others are located within a putative alternative interface. This implies that although the observed dimer structure is important for FGFR3 signaling, the mechanism of FGFR3-mediated transduction across the membrane is complex. We propose an FGFR3 signaling mechanism that is based on the solved structure, available structures of isolated soluble FGFR domains, and published biochemical and biophysical data. PubMed: 24120763DOI: 10.1016/j.str.2013.08.026 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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