2SRC

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC, IN COMPLEX WITH AMP-PNP

2SRC の概要

• エントリーDOI: 10.2210/pdb2src/pdb
• 分子名称: TYROSINE-PROTEIN KINASE SRC, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: src, tyrosine-protein kinase, phosphorylation, sh2, sh3, phosphotyrosine, proto-oncogene, phosphotransferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane: P12931
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52215.77

構造登録者

Xu, W.,Doshi, A.,Lei, M.,Eck, M.J.,Harrison, S.C. (登録日: 1998-12-29, 公開日: 1999-07-22, 最終更新日: 2024-10-30)

主引用文献

Xu, W.,Doshi, A.,Lei, M.,Eck, M.J.,Harrison, S.C.
Crystal structures of c-Src reveal features of its autoinhibitory mechanism.
Mol.Cell, 3:629-638, 1999

PubMed Abstract: Src family kinases are maintained in an assembled, inactive conformation by intramolecular interactions of their SH2 and SH3 domains. Full catalytic activity requires release of these restraints as well as phosphorylation of Tyr-416 in the activation loop. In previous structures of inactive Src kinases, Tyr-416 and flanking residues are disordered. We report here four additional c-Src structures in which this segment adopts an ordered but inhibitory conformation. The ordered activation loop forms an alpha helix that stabilizes the inactive conformation of the kinase domain, blocks the peptide substrate-binding site, and prevents Tyr-416 phosphorylation. Disassembly of the regulatory domains, induced by SH2 or SH3 ligands, or by dephosphorylation of Tyr-527, could lead to exposure and phosphorylation of Tyr-416.

PubMed: 10360179
DOI: 10.1016/S1097-2765(00)80356-1

実験手法

X-RAY DIFFRACTION (1.5 Å)