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Allosteric properties of PH domains in Arf regulatory proteins.
- Source :
-
Cellular logistics [Cell Logist] 2016 Apr 26; Vol. 6 (2), pp. e1181700. Date of Electronic Publication: 2016 Apr 26 (Print Publication: 2016). - Publication Year :
- 2016
-
Abstract
- Pleckstrin Homology (PH) domains bind phospholipids and proteins. They are critical regulatory elements of a number enzymes including guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) for Ras-superfamily guanine nucleotide binding proteins such as ADP-ribosylation factors (Arfs). Recent studies have indicated that many PH domains may bind more than one ligand cooperatively. Here we discuss the molecular basis of PH domain-dependent allosteric behavior of 2 ADP-ribosylation factor exchange factors, Grp1 and Brag2, cooperative binding of ligands to the PH domains of Grp1 and the Arf GTPase-activating protein, ASAP1, and the consequences for activity of the associated catalytic domains.
Details
- Language :
- English
- ISSN :
- 2159-2780
- Volume :
- 6
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Cellular logistics
- Publication Type :
- Academic Journal
- Accession number :
- 27294009
- Full Text :
- https://doi.org/10.1080/21592799.2016.1181700