Mechanisms of isoform-specific residue influence on GTP-bound HRas, KRas, and NRas.


Journal

Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626

Informations de publication

Date de publication:
04 10 2022
Historique:
received: 03 03 2022
revised: 04 05 2022
accepted: 01 07 2022
pubmed: 8 7 2022
medline: 12 10 2022
entrez: 7 7 2022
Statut: ppublish

Résumé

HRas, KRas, and NRas are GTPases with a common set of effectors that control many cell-signaling pathways, including proliferation through Raf kinase. Their G-domains are nearly identical in sequence, with a few isoform-specific residues that have an effect on dynamics and biochemical properties. Here, we use accelerated molecular dynamics (aMD) simulations consistent with solution x-ray scattering experiments to elucidate mechanisms through which isoform-specific residues associated with each Ras isoform affects functionally important regions connected to the active site. HRas-specific residues cluster in loop 8 to stabilize the nucleotide-binding pocket, while NRas-specific residues on helix 3 directly affect the conformations of switch I and switch II. KRas, the most globally flexible of the isoforms, shows greatest fluctuations in the switch regions enhanced by a KRas-specific residue in loop 7 and a highly dynamic loop 8 region. The analysis of isoform-specific residue effects on Ras proteins is supported by NMR experiments and is consistent with previously published biochemical data.

Identifiants

pubmed: 35794829
pii: S0006-3495(22)00551-3
doi: 10.1016/j.bpj.2022.07.005
pmc: PMC9617160
pii:
doi:

Substances chimiques

Nucleotides 0
Protein Isoforms 0
Guanosine Triphosphate 86-01-1
raf Kinases EC 2.7.11.1
Proto-Oncogene Proteins p21(ras) EC 3.6.5.2
ras Proteins EC 3.6.5.2

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

3616-3629

Informations de copyright

Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Alicia Y Volmar (AY)

Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts.

Hugo Guterres (H)

Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts.

Hao Zhou (H)

Department of Electrical and Computing Engineering, Northeastern University, Boston, Massachusetts.

Derion Reid (D)

Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts.

Spiro Pavlopoulos (S)

Department of Pharmaceutical Sciences, Northeastern University, Boston, Massachusetts.

Lee Makowski (L)

Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts; Department of Bioengineering, Northeastern University, Boston, Massachusetts.

Carla Mattos (C)

Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts. Electronic address: c.mattos@northeastern.edu.

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Classifications MeSH