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...
Үндсэн зохиолчид: | Enrique Marcos, Ramon Crehuet, Ivet Bahar |
---|---|
Формат: | Өгүүллэг |
Хэл сонгох: | English |
Хэвлэсэн: |
Public Library of Science (PLoS)
2011-09-01
|
Цуврал: | PLoS Computational Biology |
Онлайн хандалт: | http://europepmc.org/articles/PMC3182869?pdf=render |
Ижил төстэй зүйлс
-
On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm.
-н: Enrique Marcos, зэрэг
Хэвлэсэн: (2010-04-01) -
Dynamic allostery in substrate binding by human thymidylate synthase
-н: Jeffrey P Bonin, зэрэг
Хэвлэсэн: (2022-10-01) -
Allostery of atypical modulators at oligomeric G protein-coupled receptors
-н: Rabindra V. Shivnaraine, зэрэг
Хэвлэсэн: (2021-04-01) -
Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases.
-н: Nikita Chopra, зэрэг
Хэвлэсэн: (2016-03-01) -
Phosphorylation is switch of L-type pyruvate kinase allostery
-н: Faustova Ilona, зэрэг
Хэвлэсэн: (2010-04-01)