Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members.
Oligomerization is a functional requirement for many proteins. The interfacial interactions and the overall packing geometry of the individual monomers are viewed as important determinants of the thermodynamic stability and allosteric regulation of oligomers. The present study focuses on the role of...
Main Authors: | Enrique Marcos, Ramon Crehuet, Ivet Bahar |
---|---|
פורמט: | Article |
שפה: | English |
יצא לאור: |
Public Library of Science (PLoS)
2011-09-01
|
סדרה: | PLoS Computational Biology |
גישה מקוונת: | http://europepmc.org/articles/PMC3182869?pdf=render |
פריטים דומים
-
On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm.
מאת: Enrique Marcos, et al.
יצא לאור: (2010-04-01) -
Dynamic allostery in substrate binding by human thymidylate synthase
מאת: Jeffrey P Bonin, et al.
יצא לאור: (2022-10-01) -
Allostery of atypical modulators at oligomeric G protein-coupled receptors
מאת: Rabindra V. Shivnaraine, et al.
יצא לאור: (2021-04-01) -
Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases.
מאת: Nikita Chopra, et al.
יצא לאור: (2016-03-01) -
Phosphorylation is switch of L-type pyruvate kinase allostery
מאת: Faustova Ilona, et al.
יצא לאור: (2010-04-01)