1SM2

Crystal structure of the phosphorylated Interleukin-2 tyrosine kinase catalytic domain

1SM2 の概要

• エントリーDOI: 10.2210/pdb1sm2/pdb
• 分子名称: Tyrosine-protein kinase ITK/TSK, STAUROSPORINE (3 entities in total)
• 機能のキーワード: protein kinase, immunology, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane (By similarity): Q08881
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61141.91

構造登録者

Brown, K.,Long, J.M.,Vial, S.C.M.,Dedi, N.,Dunster, N.J.,Renwick, S.B.,Tanner, A.J.,Frantz, J.D.,Fleming, M.A.,Cheetham, G.M.T. (登録日: 2004-03-08, 公開日: 2004-07-16, 最終更新日: 2024-02-14)

主引用文献

Brown, K.,Long, J.M.,Vial, S.C.,Dedi, N.,Dunster, N.J.,Renwick, S.B.,Tanner, A.J.,Frantz, J.D.,Fleming, M.A.,Cheetham, G.M.
Crystal structures of interleukin-2 tyrosine kinase and their implications for the design of selective inhibitors.
J.Biol.Chem., 279:18727-18732, 2004

PubMed Abstract: Interleukin-2 tyrosine kinase, Itk, is an important member of the Tec family of non-receptor tyrosine kinases that play a central role in signaling through antigen receptors such as the T-cell receptor, B-cell receptor, and Fcepsilon. Selective inhibition of Itk may be an important way of modulating many diseases involving heightened or inappropriate activation of the immune system. In addition to an unliganded nonphophorylated Itk catalytic kinase domain, we determined the crystal structures of the phosphorylated and nonphosphorylated kinase domain bound to staurosporine, a potent broad-spectrum kinase inhibitor. These structures are useful for the design of novel, highly potent and selective Itk inhibitors and provide insight into the influence of inhibitor binding and phosphorylation on the conformation of Itk.

PubMed: 14766749
DOI: 10.1074/jbc.M400031200

実験手法

X-RAY DIFFRACTION (2.3 Å)