1a2b
From Proteopedia
(New page: 200px<br /> <applet load="1a2b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a2b, resolution 2.4Å" /> '''HUMAN RHOA COMPLEXED...) |
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| - | [[Image:1a2b. | + | [[Image:1a2b.jpg|left|200px]]<br /><applet load="1a2b" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1a2b, resolution 2.4Å" /> | caption="1a2b, resolution 2.4Å" /> | ||
'''HUMAN RHOA COMPLEXED WITH GTP ANALOGUE'''<br /> | '''HUMAN RHOA COMPLEXED WITH GTP ANALOGUE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1A2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: small g-protein]] | [[Category: small g-protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:28:12 2008'' |
Revision as of 13:28, 15 February 2008
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HUMAN RHOA COMPLEXED WITH GTP ANALOGUE
Overview
The 2.4-A resolution crystal structure of a dominantly active form of the, small guanosine triphosphatase (GTPase) RhoA, RhoAV14, complexed with the, nonhydrolyzable GTP analogue, guanosine 5'-3-O-(thio)triphosphate, (GTPgammaS), reveals a fold similar to RhoA-GDP, which has been recently, reported (Wei, Y., Zhang, Y., Derewenda, U., Liu, X., Minor, W., Nakamoto, R. K., Somlyo, A. V., Somlyo, A. P., and Derewenda, Z. S. (1997) Nat., Struct. Biol. 4, 699-703), but shows large conformational differences, localized in switch I and switch II. These changes produce hydrophobic, patches on the molecular surface of switch I, which has been suggested to, be involved in its effector binding. Compared with H-Ras and other GTPases, bound to GTP or GTP analogues, the significant conformational differences, are located in regions involving switches I and II and part of the, antiparallel beta-sheet between switches I and II. Key residues that, produce these conformational differences were identified. In addition to, these differences, RhoA contains four insertion or deletion sites with an, extra helical subdomain that seems to be characteristic of members of the, Rho family, including Rac1, but with several variations in details. These, sites also display large displacements from those of H-Ras. The, ADP-ribosylation residue, Asn41, by C3-like exoenzymes stacks on the, indole ring of Trp58 with a hydrogen bond to the main chain of Glu40. The, recognition of the guanosine moiety of GTPgammaS by the GTPase contains, water-mediated hydrogen bonds, which seem to be common in the Rho family., These structural differences provide an insight into specific interaction, sites with the effectors, as well as with modulators such as guanine, nucleotide exchange factor (GEF) and guanine nucleotide dissociation, inhibitor (GDI).
About this Structure
1A2B is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue., Ihara K, Muraguchi S, Kato M, Shimizu T, Shirakawa M, Kuroda S, Kaibuchi K, Hakoshima T, J Biol Chem. 1998 Apr 17;273(16):9656-66. PMID:9545299
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