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

Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue.

Nature - 16 Oct 1997

Rittinger K, Walker P A, Eccleston J F, Smerdon S J, Gamblin S J

Abstract excerpt

Small G proteins of the Rho family, which includes Rho, Rac and Cdc42Hs, regulate phosphorylation pathways that control a range of biological functions including cytoskeleton formation and cell proliferation. They operate as molecular switches, cycling between the biologically active GTP-bound form and the inactive GDP-bound state. Their rate of hydrolysis of GTP to GDP by virtue of their intrinsic GTPase...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cell Cycle Proteins
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to GTP-Binding Proteins

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 9338791
DOI: 10.1038/39651

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue.PMID 9338791Read ↗

How Functional Variants Reconfigure the Rac2 Conformational LandscapeSemantic proximity Read ↗

Assessing the Influence of Mutation on GTPase Transition States by Using X-ray Crystallography, 19 F NMR, and DFT Approaches.Semantic proximity Read ↗

Activation Mechanism of RhoA Caused by Constitutively Activating Mutations G14V and Q63L.Semantic proximity Read ↗

Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras.Semantic proximity Read ↗

High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop.Semantic proximity Read ↗

How Functional Variants Reconfigure the Rac2 Conformational Landscape.Semantic proximity Read ↗

Structure of an inactive conformation of GTP-bound RhoA GTPase.Semantic proximity Read ↗

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

The GTPase-activating protein Rap1GAP uses a catalytic asparagine.Semantic proximity Read ↗

Structural Dynamics of Rho GTPases.Semantic proximity Read ↗

Persistence without turnover: the RhoG G12E mutant highlights the role of nucleotide cycling in RhoG signaling.Semantic proximity Read ↗

Structural consequences of site-directed mutagenesis in flexible protein domains: NMR characterization of the L(55,56)S mutant of RhoGDI.Semantic proximity Read ↗

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