| Literature DB >> 2136935 |
Abstract
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.Mesh:
Substances:
Year: 1990 PMID: 2136935 DOI: 10.1038/343140a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962