1DJS
LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1
1DJS の概要
エントリーDOI | 10.2210/pdb1djs/pdb |
分子名称 | PROTEIN (FIBROBLAST GROWTH FACTOR RECEPTOR 2), PROTEIN (FIBROBLAST GROWTH FACTOR 1), SULFATE ION, ... (4 entities in total) |
機能のキーワード | fgfr, fgf, immunoglobulin, immune system, hormone-growth factor-receptor complex, hormone/growth factor/receptor |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Cell membrane; Single-pass type I membrane protein. Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 3: Cell membrane; Single-pass type I membrane protein. Isoform 14: Secreted. Isoform 19: Secreted: P21802 Secreted: P05230 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 40499.60 |
構造登録者 | Stauber, D.J.,Digabriele, A.D.,Hendrickson, W.A. (登録日: 1999-12-03, 公開日: 2000-01-12, 最終更新日: 2024-11-06) |
主引用文献 | Stauber, D.J.,DiGabriele, A.D.,Hendrickson, W.A. Structural interactions of fibroblast growth factor receptor with its ligands. Proc.Natl.Acad.Sci.USA, 97:49-54, 2000 Cited by PubMed Abstract: Fibroblast growth factors (FGFs) effect cellular responses by binding to FGF receptors (FGFRs). FGF bound to extracellular domains on the FGFR in the presence of heparin activates the cytoplasmic receptor tyrosine kinase through autophosphorylation. We have crystallized a complex between human FGF1 and a two-domain extracellular fragment of human FGFR2. The crystal structure, determined by multiwavelength anomalous diffraction analysis of the selenomethionyl protein, is a dimeric assemblage of 1:1 ligand:receptor complexes. FGF is bound at the junction between the two domains of one FGFR, and two such units are associated through receptor:receptor and secondary ligand:receptor interfaces. Sulfate ion positions appear to mark the course of heparin binding between FGF molecules through a basic region on receptor D2 domains. This dimeric assemblage provides a structural mechanism for FGF signal transduction. PubMed: 10618369DOI: 10.1073/pnas.97.1.49 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
