共 82 条
Sticky fingers: zinc-fingers as protein-recognition motifs
被引:338
作者:

Gamsjaeger, Roland
论文数: 0 引用数: 0
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机构:
Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia

Liew, Chu Kong
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机构:
Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia

Loughlin, Fionna E.
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机构:
Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia

Crossley, Merlin
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机构:
Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia

Mackay, Joel P.
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机构:
Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia
机构:
[1] Univ Sydney, Sch Mol & Microbial Biosci, Sydney, NSW 2006, Australia
基金:
英国医学研究理事会;
奥地利科学基金会;
关键词:
D O I:
10.1016/j.tibs.2006.12.007
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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.
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页码:63 / 70
页数:8
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