Guanosine nucleotide dissociation inhibitor
| GDP dissociation inhibitor | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
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In molecular biology, the Guanosine dissociation inhibitors (GDIs) constitute a
cdc42 by binding to its tail and preventing its insertion into membranes; hence it cannot trigger WASPs and cannot lead to nucleation of F-actin
.
The GDIs'
proteins following the transfer reaction. The mechanism of REP-1-mediated membrane
association of Rab5 is similar to that mediated by Rab GDP dissociation inhibitor (GDI). REP-1 and Rab GDI also share other functional properties, including the ability to inhibit the release of GDP and to remove Rab proteins from membranes.
The
alpha-helical
domain II.
The structural organisation of domain I is closely related to
structure at the apex of the molecule; site-directed mutagenesis has shown these regions to play a critical role in the binding of Rab proteins.[4]
References
External links
- Guanine+Nucleotide+Dissociation+Inhibitors at the U.S. National Library of Medicine Medical Subject Headings (MeSH)