1u4d

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{{STRUCTURE_1u4d| PDB=1u4d | SCENE= }}
{{STRUCTURE_1u4d| PDB=1u4d | SCENE= }}
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'''Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine'''
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===Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15308621}}
==About this Structure==
==About this Structure==
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[[Category: Stout, T J.]]
[[Category: Stout, T J.]]
[[Category: Tyrosine kinase]]
[[Category: Tyrosine kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:44:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:02:56 2008''

Revision as of 20:02, 27 July 2008

Image:1u4d.png

Template:STRUCTURE 1u4d

Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine

Template:ABSTRACT PUBMED 15308621

About this Structure

1U4D is a Single protein structure of sequence from Homo sapiens. 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

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