Macromolecular Crowding Induces a Binding Competent Transient Structure in Intrinsically Disordered Gab1.

Adaptor Proteins, Signal Transducing / chemistry Humans Intrinsically Disordered Proteins / chemistry Phosphorylation Protein Binding Protein Conformation Protein Tyrosine Phosphatase, Non-Receptor Type 11 / chemistry Tyrosine / chemistry
crowding nuclear magnetic resonance protein dynamics protein phosphorylation transient secondary structure

Journal

Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R

Informations de publication

Date de publication:
15 03 2022
Historique:
received: 26 07 2021
revised: 09 12 2021
accepted: 10 12 2021
pubmed: 21 12 2021
medline: 10 5 2022
entrez: 20 12 2021
Statut: ppublish

Résumé

Intrinsically disordered proteins (IDPs) are an important class of proteins which lack tertiary structure elements. Their dynamic properties can depend on reversible post-translational modifications and the complex cellular milieu, which provides a crowded environment. Both influences the thermodynamic stability and folding of globular proteins as well as the conformational plasticity of IDPs. Here we investigate the intrinsically disordered C-terminal region (amino acids 613-694) of human Grb2-associated binding protein 1 (Gab1), which binds to the disease-relevant Src homolog region 2 (SH2) domain-containing protein tyrosine phosphatase SHP2 (PTPN11). This binding is mediated by phosphorylation at Tyr 627 and Tyr 659 in Gab1. We characterize induced structure in Gab1

Identifiants

DOI: 10.1016/j.jmb.2021.167407 PMID: 34929201
pubmed: 34929201
pii: S0022-2836(21)00644-6
doi: 10.1016/j.jmb.2021.167407
pii:
doi:

Substances chimiques

Adaptor Proteins, Signal Transducing 0
GAB1 protein, human 0
Intrinsically Disordered Proteins 0
Tyrosine 42HK56048U
PTPN11 protein, human EC 3.1.3.48
Protein Tyrosine Phosphatase, Non-Receptor Type 11 EC 3.1.3.48

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

167407

Informations de copyright

Copyright © 2021. Published by Elsevier Ltd.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Tobias Gruber (T)

Institute of Physics, Biophysics, Martin-Luther-University of Halle-Wittenberg, Germany; Institute of Molecular Medicine, Tumor Biology, Martin-Luther-University of Halle-Wittenberg, Germany.

Marc Lewitzky (M)

Institute of Molecular Medicine, Tumor Biology, Martin-Luther-University of Halle-Wittenberg, Germany.

Lisa Machner (L)

Institute of Molecular Medicine, Tumor Biology, Martin-Luther-University of Halle-Wittenberg, Germany.

Ulrich Weininger (U)

Institute of Physics, Biophysics, Martin-Luther-University of Halle-Wittenberg, Germany.

Stephan M Feller (SM)

Institute of Molecular Medicine, Tumor Biology, Martin-Luther-University of Halle-Wittenberg, Germany. Electronic address: stephan.feller@uk-halle.de.

Jochen Balbach (J)

Institute of Physics, Biophysics, Martin-Luther-University of Halle-Wittenberg, Germany; Institute of Technical Biochemistry e.V. and Center for Structure and Dynamics of Proteins, Martin-Luther-University of Halle-Wittenberg, Germany. Electronic address: jochen.balbach@physik.uni-halle.de.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines adaptatrices de la transduction du signal › Macromolecular Crowding Induces a Binding...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Macromolecular Crowding Induces a Binding...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines intrinsèquement désordonnées › Macromolecular Crowding Induces a Binding...
questionsmedicales.fr › Métabolisme › Phosphorylation › Macromolecular Crowding Induces a Binding...
questionsmedicales.fr › Métabolisme › Liaison aux protéines › Macromolecular Crowding Induces a Binding...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Macromolecular Crowding Induces a Binding...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein Tyrosine Phosphatases › SH2 Domain-Containing Protein Tyrosine Phosphatases › Protein Tyrosine Phosphatase, Non-Receptor Type 11 › Macromolecular Crowding Induces a Binding...
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés cycliques › Acides aminés aromatiques › Tyrosine › Macromolecular Crowding Induces a Binding...