3D7U

Structural basis for the recognition of c-Src by its inactivator Csk

3D7U の概要

• エントリーDOI: 10.2210/pdb3d7u/pdb
• 関連するPDBエントリー: 3D7T
• 分子名称: Tyrosine-protein kinase CSK, Proto-oncogene tyrosine-protein kinase Src (2 entities in total)
• 機能のキーワード: csk c-src tyrosine kinase, atp-binding, kinase, membrane, nucleotide-binding, phosphoprotein, sh2 domain, sh3 domain, transferase, tyrosine-protein kinase, lipoprotein, myristate, proto-oncogene
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P41240; Cell membrane (By similarity): P00523
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122851.72

構造登録者

Levinson, N.M.,Seeliger, M.A.,Cole, P.A.,Kuriyan, J. (登録日: 2008-05-21, 公開日: 2008-08-05, 最終更新日: 2024-02-21)

主引用文献

Levinson, N.M.,Seeliger, M.A.,Cole, P.A.,Kuriyan, J.
Structural basis for the recognition of c-Src by its inactivator Csk.
Cell(Cambridge,Mass.), 134:124-134, 2008

PubMed Abstract: The catalytic activity of the Src family of tyrosine kinases is suppressed by phosphorylation on a tyrosine residue located near the C terminus (Tyr 527 in c-Src), which is catalyzed by C-terminal Src Kinase (Csk). Given the promiscuity of most tyrosine kinases, it is remarkable that the C-terminal tails of the Src family kinases are the only known targets of Csk. We have determined the crystal structure of a complex between the kinase domains of Csk and c-Src at 2.9 A resolution, revealing that interactions between these kinases position the C-terminal tail of c-Src at the edge of the active site of Csk. Csk cannot phosphorylate substrates that lack this docking mechanism because the conventional substrate binding site used by most tyrosine kinases to recognize substrates is destabilized in Csk by a deletion in the activation loop.

PubMed: 18614016
DOI: 10.1016/j.cell.2008.05.051

実験手法

X-RAY DIFFRACTION (4.111 Å)