ArticleScientific reports2017
Nucleotide Dependent Switching in Rho GTPase: Conformational Heterogeneity and Competing Molecular Interactions.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- An evolutionarily conserved salt bridge stabilizes the active site for GTP hydrolysis in Rho GTPases.The Journal of biological chemistry · 2026Article
- Article
- Structural Dynamics of Rho GTPases.Journal of molecular biology · 2025Review
- RhoA-ROCK2 signaling possesses complex pathophysiological functions in cancer progression and shows promising therapeutic potential.Cancer cell international · 2024Review
- Axonal mitochondria regulate gentle touch response through control of axonal actin dynamics.bioRxiv : the preprint server for biology · 2024Article
- Molecular mechanism of regulation of RhoA GTPase by phosphorylation of RhoGDI.Biophysical journal · 2024Article
- Wavelet coherence phase analysis decodes the universal switching mechanism of Ras GTPase superfamily.iScience · 2023Article
- Activation Mechanism of RhoA Caused by Constitutively Activating Mutations G14V and Q63L.International journal of molecular sciences · 2022Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Role of Rho guanine nucleotide exchange factors in non-small cell lung cancer.Bioengineered · 2021Article
- Structure of an inactive conformation of GTP-bound RhoA GTPase.Structure (London, England : 1993) · 2021Article
- Oncogenic mutations on Rac1 affect global intrinsic dynamics underlying GTP and PAK1 binding.Biophysical journal · 2021Article
- Conformational regulation of AP1 and AP2 clathrin adaptor complexes.Traffic (Copenhagen, Denmark) · 2019Review
- SmgGDS-607 Regulation of RhoA GTPase Prenylation Is Nucleotide-Dependent.Biochemistry · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ras superfamily of GTPases regulate myriad cellular processes through a conserved nucleotide (GTP/GDP) dependent switching mechanism. Unlike Ras family of GTPases, for the Rho GTPases, there is no clear evidence for the existence of "sub-states" such as state 1 &state 2 in the GTP bound form. To explore the nucleotide dependent conformational space of the Switch I loop and also to look for existence of state 1 like conformations in Rho GTPases, atomistic molecular dynamics and metadynamics simulations on RhoA were performed. These studies demonstrate that both the nucleotide-free state and the GDP bound "OFF" state have very similar conformations, whereas the GTP bound "ON" state has unique conformations with signatures of two intermediate states. The conformational free energy landscape for these systems suggests the presence of multiple intermediate states. Interestingly, the energetic penalty of exposing the non-polar residues in the GTP bound form is counter balanced by the favourable hydrogen bonded interactions between the γ-phosphate group of GTP with the highly conserved Tyr34 and Thr37 residues. These competing molecular interactions lead to a tuneable energy landscape of the Switch I conformation, which can undergo significant changes based on the local environment including changes upon binding to effectors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.