NDLI: A single residue can modify target-binding affinity and activity of the functional domain of the Rho-subfamily GDP dissociation inhibitors.

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A single residue can modify target-binding affinity and activity of the functional domain of the Rho-subfamily GDP dissociation inhibitors.

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A single residue can modify target-binding affinity and activity of the functional domain of the Rho-subfamily GDP dissociation inhibitors.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Platko, J. V. Adra, C. N. Cerione, R. A. Lim, B. Leonard, D. A. Shaw, R. J.
Description	Author Affiliation: Platko JV ( Department of Pharmacology, Cornell University, Ithaca, NY 14850, USA.);
Abstract	The GDP dissociation inhibitors (GDIs) represent an important class of regulatory proteins for the Rho- and Rab-subtype GTP-binding proteins. As a first step toward identifying the key functional domain(s) on the Rho-subtype GDI, truncations of the amino and carboxyl termini were performed. Deletion of the final four amino acids from the carboxyl terminus of Rho GDI or the removal of 25 amino acids from the amino terminus had no significant effect on the ability of the GDI to inhibit GDP dissociation from the Rho-like protein Cdc42Hs or on its ability to release Cdc42Hs from membrane bilayers. However, the deletion of 8 amino acids from the carboxyl terminus of Rho GDI eliminated both activities. To further test the importance of the carboxyl-terminal domain of the Rho GDI molecule, chimeras were constructed between this GDI and a related protein designated LD4, which is 67% identical to Rho GDI but is less potent by a factor of 10-20 than Rho GDI in functional assays with the Cdc42Hs protein. Two sets of chimeras were constructed that together indicated that as few as 6 amino acids near the carboxyl terminus of Rho GDI could impart full GDP dissociation inhibition and membrane dissociation activities on the LD4 molecule. Further analysis of this region by site-directed mutagenesis showed that a single change at residue 174 of LD4 to the corresponding residue of Rho GDI (i.e., Asp-174-->Ile) could impart nearly full (70%) Rho GDI activity on the LD4 molecule.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	GTP-Binding Proteins Metabolism Guanine Nucleotide Dissociation Inhibitors Guanosine Diphosphate Amino Acid Sequence Animals Aspartic Acid Drug Design Biosynthesis Isolation & Purification Glutathione Transferase Isoleucine Mice Molecular Sequence Data Mutagenesis Point Mutation Polymerase Chain Reaction Recombinant Fusion Proteins Restriction Mapping Sequence Deletion Sequence Homology, Amino Acid Rho-Specific Guanine Nucleotide Dissociation Inhibitors Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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