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1am4
From Proteopedia
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|PDB= 1am4 |SIZE=350|CAPTION= <scene name='initialview01'>1am4</scene>, resolution 2.7Å | |PDB= 1am4 |SIZE=350|CAPTION= <scene name='initialview01'>1am4</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1am4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am4 OCA], [http://www.ebi.ac.uk/pdbsum/1am4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1am4 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Smerdon, S J.]] | [[Category: Smerdon, S J.]] | ||
[[Category: Walker, P.]] | [[Category: Walker, P.]] | ||
| - | [[Category: GNP]] | ||
| - | [[Category: MG]] | ||
[[Category: complex (gtpase-activating/gtp-binding)]] | [[Category: complex (gtpase-activating/gtp-binding)]] | ||
[[Category: gtpase activation]] | [[Category: gtpase activation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:43:08 2008'' |
Revision as of 15:43, 30 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)
Overview
Small G proteins transduce signals from plasma-membrane receptors to control a wide range of cellular functions. These proteins are clustered into distinct families but all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of G proteins, which includes Cdc42Hs, activate effectors involved in the regulation of cytoskeleton formation, cell proliferation and the JNK signalling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GTPase-activating proteins (GAPs) that enhance the rate of GTP hydrolysis by up to 10(5) times. We report here the crystal structure of Cdc42Hs, with the non-hydrolysable GTP analogue GMPPNP, in complex with the GAP domain of p50rhoGAP at 2.7A resolution. In the complex Cdc42Hs interacts, mainly through its switch I and II regions, with a shallow pocket on rhoGAP which is lined with conserved residues. Arg 85 of rhoGAP interacts with the P-loop of Cdc42Hs, but from biochemical data and by analogy with the G-protein subunit G(i alpha1), we propose that it adopts a different conformation during the catalytic cycle which enables it to stabilize the transition state of the GTP-hydrolysis reaction.
About this Structure
1AM4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP., Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E, Gamblin SJ, Smerdon SJ, Nature. 1997 Aug 14;388(6643):693-7. PMID:9262406
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