1u46
From Proteopedia
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Crystal Structure of the Unphosphorylated Kinase Domain of the Tyrosine Kinase ACK1
Overview
ACK1 is a multidomain non-receptor tyrosine kinase that is an effector of, the Cdc42 GTPase. Members of the ACK family have a unique domain ordering, and are the only tyrosine kinases known to interact with Cdc42. In, contrast with many protein kinases, ACK1 has only a modest increase in, activity upon phosphorylation. We have solved the crystal structures of, the human ACK1 kinase domain in both the unphosphorylated and, phosphorylated states. Comparison of these structures reveals that ACK1, adopts an activated conformation independent of phosphorylation., Furthermore, the unphosphorylated activation loop is structured, and its, conformation resembles that seen in activated tyrosine kinases. In, addition to the apo structure, complexes are also presented with a, non-hydrolyzable nucleotide analog (adenosine, 5'-(beta,gamma-methylenetriphosphate)) and with the natural product, debromohymenialdisine, a general inhibitor of many protein kinases., Analysis of these structures reveals a typical kinase fold, a, pre-organization into the activated conformation, and an unusual, substrate-binding cleft.
About this Structure
1U46 is a Single protein structure of sequence from Homo sapiens with CL 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 the phosphorylated and unphosphorylated kinase domains of the Cdc42-associated tyrosine kinase ACK1., Lougheed JC, Chen RH, Mak P, Stout TJ, J Biol Chem. 2004 Oct 15;279(42):44039-45. Epub 2004 Aug 11. PMID:15308621
Page seeded by OCA on Mon Nov 12 19:31:28 2007
