3EAC

Crystal structure of SH2 domain of Human Csk (carboxyl-terminal src kinase), Oxidized form.

3EAC の概要

• エントリーDOI: 10.2210/pdb3eac/pdb
• 関連するPDBエントリー: 1BYG 1CSK 1K9A 3EAZ
• 分子名称: Tyrosine-protein kinase CSK (2 entities in total)
• 機能のキーワード: sh2, csk, disulfide, oxidized, reduced, atp-binding, cell membrane, kinase, membrane, nucleotide-binding, phosphoprotein, sh2 domain, sh3 domain, transferase, tyrosine-protein kinase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm : P41240
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12162.91

構造登録者

Liu, D.,Seidel, R.D.,Cowburn, D. (登録日: 2008-08-25, 公開日: 2009-11-10, 最終更新日: 2024-10-30)

主引用文献

Liu, D.,Cowburn, D.
Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.
Biophys Rep, 2:33-43, 2016

PubMed Abstract: The Src Homology 2 (SH2) domain is a structurally conserved protein domain that typically binds to a phosphorylated tyrosine in a peptide motif from the target protein. The SH2 domain of C-terminal Src kinase (Csk) contains a single disulfide bond, which is unusual for most SH2 domains. Although the global motion of SH2 domain regulates Csk function, little is known about the relationship between the disulfide bond and binding of the ligand. In this study, we combined X-ray crystallography, solution NMR, and other biophysical methods to reveal the interaction network in Csk. Denaturation studies have shown that disulfide bond contributes significantly to the stability of SH2 domain, and crystal structures of the oxidized and C122S mutant showed minor conformational changes. We further investigated the binding of SH2 domain to a phosphorylated peptide from Csk-binding protein upon reduction and oxidation using both NMR and fluorescence approaches. This work employed NMR, X-ray cryptography, and other biophysical methods to study a disulfide bond in Csk SH2 domain. In addition, this work provides in-depth understanding of the structural dynamics of Csk SH2 domain.

PubMed: 27819029
DOI: 10.1007/s41048-016-0025-4

実験手法

X-RAY DIFFRACTION (1.37 Å)