期刊
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
卷 50, 期 2, 页码 85-133出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/10409238.2014.999191
关键词
Arf; GTPase; Rab; Ran; Ras; Rho; small G protein
资金
- Medical Research Council [G0700057, MR/J007803/1] Funding Source: Medline
- MRC [G0700057, MR/J007803/1] Funding Source: UKRI
- Medical Research Council [MR/J007803/1, G0700057] Funding Source: researchfish
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 beta-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.
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