Karyopherin flexibility in nucleocytoplasmic transport

被引：170

作者：

Conti, E

Müller, CW

Stewart, M

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

[2] European Mol Biol Lab, Grenoble Outstn, F-38042 Grenoble 9, France

[3] European Mol Biol Lab, D-69117 Heidelberg, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2006年 / 16卷 / 02期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/j.sbi.2006.03.010

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：

Recent structural work on nuclear transport factors of the importin-P superfamily of karyopherins has shown that these proteins are superhelices of HEAT repeats that are able to assume different conformations in different functional states. The inherent flexibility of these helicoids facilitates the accommodation of different binding partners by an induced-fit type of mechanism. Moreover, the energy stored by distorting these molecules may partially balance binding energies to enable assembly and disassembly of their complexes with relatively small energy changes. Flexibility appears to be an intrinsic feature of such superhelices and might be functionally important not only for karyopherins and nuclear transport, but also for HEAT repeat proteins from other biological systems.

引用

收藏

页码：237 / 244

页数：8

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