This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1uix
From Proteopedia
(New page: 200px<br /><applet load="1uix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uix, resolution 1.8Å" /> '''Coiled-coil structure...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 21: | Line 21: | ||
[[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
|
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 Feb 21 15:25:04 2008
