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粘性手指:作为蛋白质识别基序的锌指结构

Sticky fingers: zinc-fingers as protein-recognition motifs.

作者信息

Gamsjaeger Roland, Liew Chu Kong, Loughlin Fionna E, Crossley Merlin, Mackay Joel P

机构信息

School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.

出版信息

Trends Biochem Sci. 2007 Feb;32(2):63-70. doi: 10.1016/j.tibs.2006.12.007. Epub 2007 Jan 8.

DOI:10.1016/j.tibs.2006.12.007
PMID:17210253
Abstract

Zinc-fingers (ZnFs) are extremely abundant in higher eukaryotes. Once considered to function exclusively as sequence-specific DNA-binding motifs, ZnFs are now known to have additional activities such as the recognition of RNA and other proteins. Here we discuss recent advances in our understanding of ZnFs as specific modules for protein recognition. Structural studies of ZnF complexes reveal considerable diversity in terms of protein partners, binding modes and affinities, and highlight the often underestimated versatility of ZnF structure and function. An appreciation of the structural features of ZnF-protein interactions will contribute to our ability to engineer and to use ZnFs with tailored protein-binding properties.

摘要

锌指(ZnF)在高等真核生物中极为丰富。锌指曾一度被认为仅作为序列特异性DNA结合基序发挥作用,如今已知其还具有其他活性,如识别RNA和其他蛋白质。在此,我们讨论了在将锌指理解为蛋白质识别的特定模块方面的最新进展。锌指复合物的结构研究揭示了在蛋白质伴侣、结合模式和亲和力方面存在相当大的差异,并突出了锌指结构和功能中常常被低估的多功能性。了解锌指与蛋白质相互作用的结构特征将有助于我们设计和使用具有定制蛋白质结合特性的锌指。

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