6pfk
PHOSPHOFRUCTOKINASE, INHIBITED T-STATEPHOSPHOFRUCTOKINASE, INHIBITED T-STATE
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedComparison 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. Structural basis of the allosteric behaviour of phosphofructokinase.,Schirmer T, Evans PR Nature. 1990 Jan 11;343(6254):140-5. PMID:2136935[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|