1sm2
From Proteopedia
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Crystal structure of the phosphorylated Interleukin-2 tyrosine kinase catalytic domain
Contents |
Overview
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.
Disease
Known disease associated with this structure: Polyhydramnios, megalencephaly, and symptomatic epilepsy OMIM:[608626]
About this Structure
1SM2 is a Single protein structure of sequence from Homo sapiens with STU as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Crystal structures of interleukin-2 tyrosine kinase and their implications for the design of selective inhibitors., Brown K, Long JM, Vial SC, Dedi N, Dunster NJ, Renwick SB, Tanner AJ, Frantz JD, Fleming MA, Cheetham GM, J Biol Chem. 2004 Apr 30;279(18):18727-32. Epub 2004 Feb 6. PMID:14766749
Page seeded by OCA on Mon Nov 12 19:15:23 2007
