1uix: Difference between revisions
New page: left|200px<br /><applet load="1uix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uix, resolution 1.8Å" /> '''Coiled-coil structure... |
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[[Image:1uix.jpg|left|200px]]<br /><applet load="1uix" size=" | [[Image:1uix.jpg|left|200px]]<br /><applet load="1uix" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1uix, resolution 1.8Å" /> | caption="1uix, resolution 1.8Å" /> | ||
'''Coiled-coil structure of the RhoA-binding domain in Rho-kinase'''<br /> | '''Coiled-coil structure of the RhoA-binding domain in Rho-kinase'''<br /> | ||
==Overview== | ==Overview== | ||
Rho-kinase is a serine/threonine protein kinase that regulates | 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== | ==About this Structure== | ||
1UIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | 1UIX is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:04 2008'' | ||
Revision as of 13:25, 21 February 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
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