期刊
STRUCTURE
卷 21, 期 8, 页码 1284-1297出版社
CELL PRESS
DOI: 10.1016/j.str.2013.06.016
关键词
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资金
- Association pour la Recherche contre le Cancer [SFI20101201744, SFI20121205592]
- Agence Nationale pour la Recherche [ANR-08-JCJC-0110-01]
- Science Foundation Ireland Investigator Award [07/IN.1/B975]
- Agence Nationale de la Recherche (ANR) [ANR-08-JCJC-0110] Funding Source: Agence Nationale de la Recherche (ANR)
- Science Foundation Ireland (SFI) [07/IN.1/B975] Funding Source: Science Foundation Ireland (SFI)
Arf and Rab proteins, members of small GTPases superfamily, localize to specific subcellular compartments and regulate intracellular trafficking. To carry out their cellular functions, Arfs/Rabs interact with numerous and structurally diverse effector proteins. Over the years, a number of Arf/Rab:effector complexes have been crystallized and their structures reveal shared binding modes including alpha-helical packing, beta-beta complementation, and heterotetrameric assemblies. We review available structural information and provide a framework for in-depth analysis of complexes. The unifying features that we identify are organized into a classification scheme for different modes of Arf/Rab:effector interactions, which includes all-alpha-helical, mixed alpha-helical, beta-beta zipping, and bivalent modes of binding. Additionally, we highlight structural determinants that are the basis of effector specificity. We conclude by expanding on functional implications that are emerging from available structural information under our proposed classification scheme.
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