1u4d

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[[Image:1u4d.gif|left|200px]]
[[Image:1u4d.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1u4d |SIZE=350|CAPTION= <scene name='initialview01'>1u4d</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1u4d", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DBQ:DEBROMOHYMENIALDISINE'>DBQ</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= ACK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1u4d| PDB=1u4d | SCENE= }}
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|RELATEDENTRY=[[1u46|1U46]], [[1u54|1U54]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u4d OCA], [http://www.ebi.ac.uk/pdbsum/1u4d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u4d RCSB]</span>
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}}
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'''Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine'''
'''Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine'''
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[[Category: Mak, P.]]
[[Category: Mak, P.]]
[[Category: Stout, T J.]]
[[Category: Stout, T J.]]
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[[Category: tyrosine kinase]]
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[[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 Mon Mar 31 00:05:15 2008''
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Revision as of 07:44, 3 May 2008

Template:STRUCTURE 1u4d

Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine


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

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 Page seeded by OCA on Sat May 3 10:44:53 2008

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