1uix: Difference between revisions
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'''Coiled-coil structure of the RhoA-binding domain in Rho-kinase''' | {{Structure | ||
|PDB= 1uix |SIZE=350|CAPTION= <scene name='initialview01'>1uix</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''Coiled-coil structure of the RhoA-binding domain in Rho-kinase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1UIX is a [ | 1UIX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UIX OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12954645 12954645] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:32:36 2008'' | ||
Revision as of 12:32, 20 March 2008
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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 Thu Mar 20 14:32:36 2008
