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Crit Rev Biochem Mol Biol. 2015 Mar-Apr;50(2):85-133. doi: 10.3109/10409238.2014.999191. Epub 2015 Apr 1.

Structures of Ras superfamily effector complexes: What have we learnt in two decades?

Author information

1
Department of Biochemistry, University of Cambridge , Cambridge , UK.

Abstract

The Ras superfamily small G proteins are master regulators of a diverse range of cellular processes and act via downstream effector molecules. The first structure of a small G protein-effector complex, that of Rap1A with c-Raf1, was published 20 years ago. Since then, the structures of more than 60 small G proteins in complex with their effectors have been published. These effectors utilize a diverse array of structural motifs to interact with the G protein fold, which we have divided into four structural classes: intermolecular β-sheets, helical pairs, other interactions, and pleckstrin homology (PH) domains. These classes and their representative structures are discussed and a contact analysis of the interactions is presented, which highlights the common effector-binding regions between and within the small G protein families.

KEYWORDS:

Arf; GTPase; Rab; Ran; Ras; Rho; small G protein

PMID:
25830673
DOI:
10.3109/10409238.2014.999191
[Indexed for MEDLINE]

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