STRUCTURAL BASIS OF THE ALLOSTERIC BEHAVIOR OF PHOSPHOFRUCTOKINASE

被引：245

作者：

SCHIRMER, T ^{[1
]}

EVANS, PR ^{[1
]}

机构：

[1] MRC,MOLEC BIOL LAB,CAMBRIDGE CB2 2QH,ENGLAND

来源：

NATURE | 1990年 / 343卷 / 6254期

关键词：

D O I：

10.1038/343140a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Comparison between the crystal structures of low-and high-affinity forms of phosphofructokinase shows a close coupling between the change of quaternary structure and local changes triggered by binding of the allosteric effectors. These concerted changes link all the substrate and effector sites in the tetramer, and explain the change of affinity for the cooperative substrate. © 1990 Nature Publishing Group.

引用

页码：140 / 145

页数：6

共 20 条

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