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...

Bibliografski detalji
Glavni autori:	Enrique Marcos, Ramon Crehuet, Ivet Bahar
Format:	Članak
Jezik:	English
Izdano:	Public Library of Science (PLoS) 2011-09-01
Serija:	PLoS Computational Biology
Online pristup:	http://europepmc.org/articles/PMC3182869?pdf=render

Slični predmeti

On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm.
od: Enrique Marcos, i dr.
Izdano: (2010-04-01)

Dynamic allostery in substrate binding by human thymidylate synthase
od: Jeffrey P Bonin, i dr.
Izdano: (2022-10-01)

Allostery of atypical modulators at oligomeric G protein-coupled receptors
od: Rabindra V. Shivnaraine, i dr.
Izdano: (2021-04-01)

Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases.
od: Nikita Chopra, i dr.
Izdano: (2016-03-01)

Phosphorylation is switch of L-type pyruvate kinase allostery
od: Faustova Ilona, i dr.
Izdano: (2010-04-01)

ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.
od: Ignacio J General, i dr.
Izdano: (2014-05-01)

Computational modeling of cAMP-dependent protein kinase allostery
od: Andrei Izvolski, i dr.
Izdano: (2023-11-01)

Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery
od: Brandall L. Ingle, i dr.
Izdano: (2019-01-01)

Editorial: Understanding Protein Dynamics, Binding and Allostery for Drug Design
od: Guang Hu, i dr.
Izdano: (2021-04-01)

Kinase Domain Is a Dynamic Hub for Driving LRRK2 Allostery
od: Susan S. Taylor, i dr.
Izdano: (2020-10-01)

Wandering about allostery
od: Maurizio Brunori
Izdano: (2024-08-01)

Decoding the mechanisms of allostery
od: Saif Khan, i dr.
Izdano: (2023-06-01)

Modeling Spatial Correlation of DNA Deformation: DNA Allostery in Protein Binding
od: Xu, Xinliang, i dr.
Izdano: (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
od: Hüseyin Ilgü, i dr.
Izdano: (2021-08-01)

Allostery can convert binding free energies into concerted domain motions in enzymes
od: Nicole Stéphanie Galenkamp, i dr.
Izdano: (2024-11-01)

Ligand structure controlled allostery in cAMP-dependent protein kinase catalytic subunit
od: Kuznetsov Aleksei, i dr.
Izdano: (2009-06-01)

Is allostery a fuzzy concept?
od: Veronica Morea, i dr.
Izdano: (2024-07-01)

Convergent allostery in ribonucleotide reductase
od: William C. Thomas, i dr.
Izdano: (2019-06-01)

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

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain
od: Aprile, F, i dr.
Izdano: (2013)

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.
od: Francesco A Aprile, i dr.
Izdano: (2013-01-01)

Deconstructing allostery by computational assessment of the binding determinants of allosteric PTP1B modulators
od: Adele Hardie, i dr.
Izdano: (2023-06-01)

GMP Synthetase: Allostery, Structure, and Function
od: Lionel Ballut, i dr.
Izdano: (2023-09-01)

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

NMR Methods to Study Dynamic Allostery.
od: Sarina Grutsch, i dr.
Izdano: (2016-03-01)

Ack1: activation and regulation by allostery.
od: Ketan S Gajiwala, i dr.
Izdano: (2013-01-01)

Possible mechanism and clinical potentials of allostery
od: Peixin Huang, i dr.
Izdano: (2014-12-01)

Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding.
od: Kotaka, M, i dr.
Izdano: (2006)

Author Correction: Allostery can convert binding free energies into concerted domain motions in enzymes
od: Nicole Stéphanie Galenkamp, i dr.
Izdano: (2025-01-01)

Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding
od: Scacioc, A, i dr.
Izdano: (2018)

Designing allostery-inspired response in mechanical networks
od: Rocks, Jason W., i dr.
Izdano: (2017)

Investigating potential allostery in the transcription factor CREB
od: Chung, NL
Izdano: (2020)

HIV-1 Envelope Conformation, Allostery, and Dynamics
od: Ashley Lauren Bennett, i dr.
Izdano: (2021-05-01)

Allostery and Epistasis: Emergent Properties of Anisotropic Networks
od: Paul Campitelli, i dr.
Izdano: (2020-06-01)

Structural Basis for Allostery in PLP-dependent Enzymes
od: Jenny U. Tran, i dr.
Izdano: (2022-04-01)

Insights into the molecular mechanism of allostery in Hsp70s
od: Matthias Peter Mayer, i dr.
Izdano: (2015-10-01)

A unified view of "how allostery works".
od: Chung-Jung Tsai, i dr.
Izdano: (2014-02-01)

Allostery through DNA drives phenotype switching
od: Gabriel Rosenblum, i dr.
Izdano: (2021-05-01)

Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions
od: Noboru Ishiyama, i dr.
Izdano: (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
od: Sarah Norklit Roed, i dr.
Izdano: (2012-05-01)