Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members.

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...

Полное описание

Библиографические подробности
Главные авторы:	Enrique Marcos, Ramon Crehuet, Ivet Bahar
Формат:	Статья
Язык:	English
Опубликовано:	Public Library of Science (PLoS) 2011-09-01
Серии:	PLoS Computational Biology
Online-ссылка:	http://europepmc.org/articles/PMC3182869?pdf=render

Схожие документы

On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm.
по: Enrique Marcos, и др.
Опубликовано: (2010-04-01)

Dynamic allostery in substrate binding by human thymidylate synthase
по: Jeffrey P Bonin, и др.
Опубликовано: (2022-10-01)

Allostery of atypical modulators at oligomeric G protein-coupled receptors
по: Rabindra V. Shivnaraine, и др.
Опубликовано: (2021-04-01)

Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases.
по: Nikita Chopra, и др.
Опубликовано: (2016-03-01)

Phosphorylation is switch of L-type pyruvate kinase allostery
по: Faustova Ilona, и др.
Опубликовано: (2010-04-01)

ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.
по: Ignacio J General, и др.
Опубликовано: (2014-05-01)

Computational modeling of cAMP-dependent protein kinase allostery
по: Andrei Izvolski, и др.
Опубликовано: (2023-11-01)

Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery
по: Brandall L. Ingle, и др.
Опубликовано: (2019-01-01)

Editorial: Understanding Protein Dynamics, Binding and Allostery for Drug Design
по: Guang Hu, и др.
Опубликовано: (2021-04-01)

Kinase Domain Is a Dynamic Hub for Driving LRRK2 Allostery
по: Susan S. Taylor, и др.
Опубликовано: (2020-10-01)

Wandering about allostery
по: Maurizio Brunori
Опубликовано: (2024-08-01)

Decoding the mechanisms of allostery
по: Saif Khan, и др.
Опубликовано: (2023-06-01)

Modeling Spatial Correlation of DNA Deformation: DNA Allostery in Protein Binding
по: Xu, Xinliang, и др.
Опубликовано: (2014)

High-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding
по: Hüseyin Ilgü, и др.
Опубликовано: (2021-08-01)

Allostery can convert binding free energies into concerted domain motions in enzymes
по: Nicole Stéphanie Galenkamp, и др.
Опубликовано: (2024-11-01)

Ligand structure controlled allostery in cAMP-dependent protein kinase catalytic subunit
по: Kuznetsov Aleksei, и др.
Опубликовано: (2009-06-01)

Is allostery a fuzzy concept?
по: Veronica Morea, и др.
Опубликовано: (2024-07-01)

Convergent allostery in ribonucleotide reductase
по: William C. Thomas, и др.
Опубликовано: (2019-06-01)

The role of the N domain in substrate binding, oligomerization, and allosteric regulation of the AAA+ Lon protease
по: Wohlever, Matthew L
Опубликовано: (2013)

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain
по: Aprile, F, и др.
Опубликовано: (2013)

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.
по: Francesco A Aprile, и др.
Опубликовано: (2013-01-01)

Deconstructing allostery by computational assessment of the binding determinants of allosteric PTP1B modulators
по: Adele Hardie, и др.
Опубликовано: (2023-06-01)

GMP Synthetase: Allostery, Structure, and Function
по: Lionel Ballut, и др.
Опубликовано: (2023-09-01)

Dynamic allostery in thrombin—a review
по: Elizabeth A. Komives
Опубликовано: (2023-06-01)

NMR Methods to Study Dynamic Allostery.
по: Sarina Grutsch, и др.
Опубликовано: (2016-03-01)

Ack1: activation and regulation by allostery.
по: Ketan S Gajiwala, и др.
Опубликовано: (2013-01-01)

Possible mechanism and clinical potentials of allostery
по: Peixin Huang, и др.
Опубликовано: (2014-12-01)

Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding.
по: Kotaka, M, и др.
Опубликовано: (2006)

Author Correction: Allostery can convert binding free energies into concerted domain motions in enzymes
по: Nicole Stéphanie Galenkamp, и др.
Опубликовано: (2025-01-01)

Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding
по: Scacioc, A, и др.
Опубликовано: (2018)

Designing allostery-inspired response in mechanical networks
по: Rocks, Jason W., и др.
Опубликовано: (2017)

Investigating potential allostery in the transcription factor CREB
по: Chung, NL
Опубликовано: (2020)

HIV-1 Envelope Conformation, Allostery, and Dynamics
по: Ashley Lauren Bennett, и др.
Опубликовано: (2021-05-01)

Allostery and Epistasis: Emergent Properties of Anisotropic Networks
по: Paul Campitelli, и др.
Опубликовано: (2020-06-01)

Structural Basis for Allostery in PLP-dependent Enzymes
по: Jenny U. Tran, и др.
Опубликовано: (2022-04-01)

Insights into the molecular mechanism of allostery in Hsp70s
по: Matthias Peter Mayer, и др.
Опубликовано: (2015-10-01)

A unified view of "how allostery works".
по: Chung-Jung Tsai, и др.
Опубликовано: (2014-02-01)

Allostery through DNA drives phenotype switching
по: Gabriel Rosenblum, и др.
Опубликовано: (2021-05-01)

Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions
по: Noboru Ishiyama, и др.
Опубликовано: (2018-11-01)

Receptor oligomerization in family B1 of G-protein-coupled receptors: Focus on BRET investigations and the link between GPCR oligomerization and binding cooperativity
по: Sarah Norklit Roed, и др.
Опубликовано: (2012-05-01)