1cc0: Difference between revisions

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[[Image:1cc0.jpg|left|200px]]
{{Seed}}
[[Image:1cc0.png|left|200px]]


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{{STRUCTURE_1cc0|  PDB=1cc0  |  SCENE=  }}  
{{STRUCTURE_1cc0|  PDB=1cc0  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX'''
===CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX===




==Overview==
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Like all Rho (Ras homology) GTPases, RhoA functions as a molecular switch in cell signaling, alternating between GTP- and GDP-bound states, with its biologically inactive GDP-bound form maintained as a cytosolic complex with RhoGDI (guanine nucleotide-exchange inhibitor). The crystal structures of RhoA-GDP and of the C-terminal immunoglobulin-like domain of RhoGDI (residues 67-203) are known, but the mechanism by which the two proteins interact is not known. The functional human RhoA-RhoGDI complex has been expressed in yeast and crystallized (P6(5)22, unit-cell parameters a = b = 139, c = 253 A, two complexes in the asymmetric unit). Although diffraction from these crystals extends to 3.5 A and is highly anisotropic, the experimentally phased (MAD plus MIR) electron-density map was adequate to reveal the mutual disposition of the two molecules. The result was validated by molecular-replacement calculations when data were corrected for anisotropy. Furthermore, the N-terminus of RhoGDI (the region involved in inhibition of nucleotide exchange) can be identified in the electron-density map: it is bound to the switch I and switch II regions of RhoA, occluding an epitope which binds Dbl-like nucleotide-exchange factors. The entrance of the hydrophobic pocket of RhoGDI is 25 A from the last residue in the RhoA model, with its C-terminus oriented to accommodate the geranylgeranyl group without conformational change in RhoA.
The line below this paragraph, {{ABSTRACT_PUBMED_10489445}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_10489445}}


==About this Structure==
==About this Structure==
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[[Category: G-protein]]
[[Category: G-protein]]
[[Category: Rho gtpase]]
[[Category: Rho gtpase]]
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