Title : Structure-activity relationships in flexible protein domains: regulation of rho GTPases by RhoGDI and D4 GDI.

Pub. Date : 2001 Jan 5

PMID : 11114252






2 Functional Relationships(s)
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1 These studies show that the first 30 amino acid residues are not required for inhibition of GDP dissociation but appear to be important for GTP hydrolysis, whilst removal of the first 41 residues completely abolish the ability of RhoGDI to inhibit GDP dissociation. Guanosine Triphosphate Rho GDP dissociation inhibitor alpha Homo sapiens
2 The combination of structural and functional studies allows us to explain why RhoGDI and D4GDI are able to interact in similar ways with the guanosine 5"-diphosphate-bound GTPase, but differ in their ability to regulate GTP-bound forms; these functional differences are attributed to the conformational differences of the N-terminal domains of the guanosine 5"-diphosphate dissociation inhibitors. Guanosine Triphosphate Rho GDP dissociation inhibitor alpha Homo sapiens