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...
المؤلفون الرئيسيون: | Enrique Marcos, Ramon Crehuet, Ivet Bahar |
---|---|
التنسيق: | مقال |
اللغة: | English |
منشور في: |
Public Library of Science (PLoS)
2011-09-01
|
سلاسل: | PLoS Computational Biology |
الوصول للمادة أونلاين: | http://europepmc.org/articles/PMC3182869?pdf=render |
مواد مشابهة
-
On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm.
حسب: Enrique Marcos, وآخرون
منشور في: (2010-04-01) -
Dynamic allostery in substrate binding by human thymidylate synthase
حسب: Jeffrey P Bonin, وآخرون
منشور في: (2022-10-01) -
Allostery of atypical modulators at oligomeric G protein-coupled receptors
حسب: Rabindra V. Shivnaraine, وآخرون
منشور في: (2021-04-01) -
Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases.
حسب: Nikita Chopra, وآخرون
منشور في: (2016-03-01) -
Phosphorylation is switch of L-type pyruvate kinase allostery
حسب: Faustova Ilona, وآخرون
منشور في: (2010-04-01)