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Article

Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease.

Proceedings of the National Academy of Sciences of the United States of America - 27 Feb 2007

Beasley Steven A, Hristova Ventzislava A, Shaw Gary S

Abstract excerpt

Mutations in Parkin are one of the predominant hereditary factors found in patients suffering from autosomal recessive juvenile Parkinsonism. Parkin is a member of the E3 ubiquitin ligase family that is defined by a tripartite RING1-in-between-ring (IBR)-RING2 motif. In Parkin, the IBR domain has...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 17360614
DOI: 10.1073/pnas.0610548104
PMCID: PMC1805599

Genes

RING1
SIM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-17360614-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease.PMID 17360614Read ↗

Mutational Impact on "in-Between-Ring" (IBR) Domain of PARKIN on Protein Stability and Function.Semantic proximity Read ↗

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Identification of a Novel Zn2+-binding Domain in the Autosomal Recessive Juvenile Parkinson-related E3 Ligase ParkinSemantic proximity Read ↗

Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases.Semantic proximity Read ↗

Structural analysis of the effects of mutations in Ubl domain of Parkin leading to Parkinson's disease.Semantic proximity Read ↗

A molecular explanation for the recessive nature of parkin-linked Parkinson's disease.Semantic proximity Read ↗

Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING.Semantic proximity Read ↗

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A Ubl/ubiquitin switch in the activation of ParkinSemantic proximity Read ↗

Structure of parkin reveals mechanisms for ubiquitin ligase activation.Semantic proximity Read ↗

Mechanism of phospho-Ubls' specificity and conformational changes that regulate Parkin activity.Semantic proximity Read ↗

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