2PSQ

Crystal Structure of Unphosphorylated Unactivated Wild Type FGF Receptor 2 (FGFR2) Kinase Domain

2PSQ の概要

• エントリーDOI: 10.2210/pdb2psq/pdb
• 関連するPDBエントリー: 1GJO 1OEC 2PVF 2PVY 2PWL 2PY3 2PZ5 2PZP 2PZR 2Q0B
• 分子名称: Fibroblast growth factor receptor 2, SULFATE ION (3 entities in total)
• 機能のキーワード: kinase domain fold consisting of n- and c-lobes, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein. Isoform 14: Secreted. Isoform 19: Secreted: P21802
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84660.93

構造登録者

Chen, H.,Mohammadi, M. (登録日: 2007-05-07, 公開日: 2007-09-25, 最終更新日: 2023-08-30)

主引用文献

Chen, H.,Ma, J.,Li, W.,Eliseenkova, A.V.,Xu, C.,Neubert, T.A.,Miller, W.T.,Mohammadi, M.
A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.
Mol.Cell, 27:717-730, 2007

PubMed Abstract: Activating mutations in the tyrosine kinase domain of receptor tyrosine kinases (RTKs) cause cancer and skeletal disorders. Comparison of the crystal structures of unphosphorylated and phosphorylated wild-type FGFR2 kinase domains with those of seven unphosphorylated pathogenic mutants reveals an autoinhibitory "molecular brake" mediated by a triad of residues in the kinase hinge region of all FGFRs. Structural analysis shows that many other RTKs, including PDGFRs, VEGFRs, KIT, CSF1R, FLT3, TEK, and TIE, are also subject to regulation by this brake. Pathogenic mutations activate FGFRs and other RTKs by disengaging the brake either directly or indirectly.

PubMed: 17803937
DOI: 10.1016/j.molcel.2007.06.028

実験手法

X-RAY DIFFRACTION (2.4 Å)