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

Novel LRR-ROC Motif That Links the N- and C-terminal Domains in LRRK2 Undergoes an Order-Disorder Transition Upon Activation.

Journal of molecular biology - 15 Jun 2023

Weng Jui-Hung, Trilling Chiara R, Kaila Sharma Pallavi, Störmer Eliza, Wu Jian, Herberg Friedrich W, Taylor Susan S

Abstract excerpt

Mutations in LRRK2, a large multi-domain protein kinase, create risk factors for Parkinson's Disease (PD). LRRK2 has seven well-folded domains that include three N-terminal scaffold domains (NtDs) and four C-terminal domains (CtDs). In full-length inactive LRRK2 there is an additional well-folded motif, the LRR-ROC Linker, that lies between the NtDs and the CtDs. This motif, which is stabilized by hydrophobic...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to GTP Phosphohydrolases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Leucine-Rich Repeat Serine-Threonine Protein Kinase-2

Share to Mutation

Share to Parkinson Disease

Share to Phosphorylation

Source

Identifiers

PMID: 36764356
DOI: 10.1016/j.jmb.2023.167999

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

Novel LRR-ROC Motif That Links the N- and C-terminal Domains in LRRK2 Undergoes an Order-Disorder Transition Upon Activation.PMID 36764356Read ↗

Conformation and dynamics of the kinase domain drive subcellular location and activation of LRRK2Semantic proximity Read ↗

Structure of LRRK1 and mechanisms of autoinhibition and activationSemantic proximity Read ↗

R1398 is the GTP-𝛾-phosphate sensor that drives the ROC G-domain switching mechanism unique to Parkinson's disease-associated LRRK2Semantic proximity Read ↗

Structure of LRRK1 and mechanisms of autoinhibition and activation.Semantic proximity Read ↗

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant.Semantic proximity Read ↗

LRRK2 Structure-Based Activation Mechanism and Pathogenesis.Semantic proximity Read ↗

Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPaseSemantic proximity Read ↗

Structural and biochemical basis of ROC-dependent activation of LRRK2Semantic proximity Read ↗

The structural basis for LRRK2’s activation and autoinhibitionSemantic proximity Read ↗

Markov State Models and Molecular Dynamics Simulations Provide Understanding of the Nucleotide-Dependent Dimerization-Based Activation of LRRK2 ROC Domain.Semantic proximity Read ↗

Structural biology of the LRRK2 GTPase and kinase domains: implications for regulationSemantic proximity Read ↗

A revised 1.6 Å structure of the GTPase domain of the Parkinson’s disease-associated protein LRRK2 provides insights into mechanismsSemantic proximity Read ↗

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