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...
Κύριοι συγγραφείς: | Enrique Marcos, Ramon Crehuet, Ivet Bahar |
---|---|
Μορφή: | Άρθρο |
Γλώσσα: | English |
Έκδοση: |
Public Library of Science (PLoS)
2011-09-01
|
Σειρά: | PLoS Computational Biology |
Διαθέσιμο Online: | http://europepmc.org/articles/PMC3182869?pdf=render |
Παρόμοια τεκμήρια
-
On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm.
ανά: Enrique Marcos, κ.ά.
Έκδοση: (2010-04-01) -
Dynamic allostery in substrate binding by human thymidylate synthase
ανά: Jeffrey P Bonin, κ.ά.
Έκδοση: (2022-10-01) -
Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases.
ανά: Nikita Chopra, κ.ά.
Έκδοση: (2016-03-01) -
ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.
ανά: Ignacio J General, κ.ά.
Έκδοση: (2014-05-01) -
Computational modeling of cAMP-dependent protein kinase allostery
ανά: Andrei Izvolski, κ.ά.
Έκδοση: (2023-11-01)