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1uix

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uix OCA], [http://www.ebi.ac.uk/pdbsum/1uix PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uix RCSB]</span>
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'''Coiled-coil structure of the RhoA-binding domain in Rho-kinase'''
'''Coiled-coil structure of the RhoA-binding domain in Rho-kinase'''
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[[Category: Maesaki, R.]]
[[Category: Maesaki, R.]]
[[Category: Shimizu, T.]]
[[Category: Shimizu, T.]]
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[[Category: coiled-coil]]
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[[Category: Coiled-coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:17:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:10:56 2008''
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Revision as of 08:17, 3 May 2008

Image:1uix.jpg

Template:STRUCTURE 1uix

Coiled-coil structure of the RhoA-binding domain in Rho-kinase


Overview

Rho-kinase is a serine/threonine protein kinase that regulates cytoskeletal events in cells. The enzyme activity of Rho-kinase is auto-inhibited in the free state but is activated through direct binding to the small GTPase Rho in the GTP-bound form. The crystal structure of the Rho-binding domain (RhoBD) of Rho-kinase has been determined at 1.8-A resolution by the multi-wavelength anomalous dispersion technique. The structure shows that RhoBD dimerizes to form a parallel coiled-coil with long consecutive alpha-helices extended to approximately 97 A and suggests that free Rho-kinase can also form a dimer through parallel self-association. At the middle region of the coiled-coil, the polypeptide chains are flexible and display loose "knobs-into-holes" packing of the side chains from both chains. RhoBD residues that have been shown to be critical for Rho-binding are spread in the positively charged C-terminal region. The parallel coiled-coil structure of our Rho-kinase RhoBD in the free form is different from the anti-parallel coiled-coil structure of RhoBD of protein kinase N when complexed with RhoA. Implications derived from these structural studies in relation to the mechanism of Rho-kinase activation will be addressed with previously reported experimental data.

About this Structure

1UIX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Parallel coiled-coil association of the RhoA-binding domain in Rho-kinase., Shimizu T, Ihara K, Maesaki R, Amano M, Kaibuchi K, Hakoshima T, J Biol Chem. 2003 Nov 14;278(46):46046-51. Epub 2003 Sep 3. PMID:12954645 Page seeded by OCA on Sat May 3 11:17:41 2008

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