Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

GTP-Bound N-Ras Conformational States and Substates Are Modulated by Membrane and Point Mutation.

International journal of molecular sciences - 24 Jan 2024

Farcas Alexandra, Janosi Lorant

Abstract excerpt

Oncogenic Ras proteins are known to present multiple conformational states, as reported by the great variety of crystallographic structures. The GTP-bound states are grouped into two main states: the "inactive" state 1 and the "active" state 2. Recent reports on H-Ras have shown that state 2 exhibits two substates, directly related to the orientation of Tyr32: toward the GTP-bound pocket and outwards. In this...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Guanine Nucleotide Exchange Factors
Share to Guanosine Triphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Point Mutation

Share to Proto-Oncogene Proteins p21(ras)

Share to ras Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 38338709
DOI: 10.3390/ijms25031430
PMCID: PMC11154311

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

GTP-Bound N-Ras Conformational States and Substates Are Modulated by Membrane and Point Mutation.PMID 38338709Read ↗

Conformational Dynamics Allows Sampling of an "Active-like" State by Oncogenic K-Ras-GDP.Semantic proximity Read ↗

Mutational landscape of K-Ras substitutions at 12th position-a systematic molecular dynamics approach.Semantic proximity Read ↗

Structural insight into the rearrangement of the switch I region in GTP-bound G12A K-Ras.Semantic proximity Read ↗

K-Ras Populates Conformational States Differently from Its Isoform H-Ras and Oncogenic Mutant K-RasG12D.Semantic proximity Read ↗

The Structural Basis of Oncogenic Mutations G12, G13 and Q61 in Small GTPase K-Ras4B.Semantic proximity Read ↗

Identification of functional substates of KRas during GTP hydrolysis with enhanced sampling simulations.Semantic proximity Read ↗

GTP Binding and Oncogenic Mutations May Attenuate Hypervariable Region (HVR)-Catalytic Domain Interactions in Small GTPase K-Ras4B, Exposing the Effector Binding Site.Semantic proximity Read ↗

Delineating the RAS Conformational Landscape.Semantic proximity Read ↗

Dynamically encoded reactivity of Ras enzymes: opening new frontiers for drug discovery.Semantic proximity Read ↗

The Importance of Mg2+ -Free State in Nucleotide Exchange of Oncogenic K-Ras Mutants.Semantic proximity Read ↗

Oncogenic G12D mutation alters local conformations and dynamics of K-RasSemantic proximity Read ↗

Distinct dynamics and interaction patterns in H- and K-Ras oncogenic P-loop mutants.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.