Related Experiment Video
Updated: Mar 19, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
Published on: October 8, 2015
Allosteric properties of PH domains in Arf regulatory proteins
Neeladri Sekhar Roy1, Marielle E Yohe2, Paul A Randazzo1
1Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.
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.
More Related Videos
07:41A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
Published on: February 20, 2018
10:19Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
Published on: January 24, 2025
Related Concept Videos
GTPases and their Regulation
Large G-proteins,...
GTPases and their Regulation
Activation and Inactivation of G Proteins
Amplifying Signals via Enzymatic Cascade
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
GPCRs Regulate Adenylyl Cylase Activity