共 64 条
Natively unfolded proteins
被引:569
作者:

Fink, AL
论文数: 0 引用数: 0
h-index: 0
机构:
Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA
机构:
[1] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA
关键词:
D O I:
10.1016/j.sbi.2005.01.002
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:
It is now clear that a significant fraction of eukaryotic genomes encode proteins with substantial regions of disordered structure. In spite of the lack of structure, these proteins nevertheless are functional; many are involved in critical steps of the cell cycle and regulatory processes. In general, intrinsically disordered proteins interact with a target ligand (often DNA) and undergo a structural transition to a folded form when bound. Several features of intrinsically disordered proteins make them well suited to interacting with multiple targets and to cell regulation. New algorithms have been developed to identify disordered regions of proteins and have demonstrated their presence in cancer-associated proteins and proteins regulated by phosphorylation.
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页码:35 / 41
页数:7
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共 64 条
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