Structural basis of the allosteric behaviour of phosphofructokinase.

Article Details

Citation

Schirmer T, Evans PR

Structural basis of the allosteric behaviour of phosphofructokinase.

Nature. 1990 Jan 11;343(6254):140-5.

PubMed ID
2136935 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
ATP-dependent 6-phosphofructokinaseP00512Details