1am4: Difference between revisions

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[[Image:1am4.gif|left|200px]]
{{Seed}}
[[Image:1am4.png|left|200px]]


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{{STRUCTURE_1am4|  PDB=1am4  |  SCENE=  }}  
{{STRUCTURE_1am4|  PDB=1am4  |  SCENE=  }}  


'''COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)'''
===COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9262406}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9262406}}


==About this Structure==
==About this Structure==
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[[Category: Walker, P.]]
[[Category: Walker, P.]]
[[Category: Gtpase activation]]
[[Category: Gtpase activation]]
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