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

Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin.

Structure (London, England : 1993) - 4 Mar 2014

Gao Yong-Guang, Yang Hui, Zhao Jian, Jiang Ya-Jun, Hu Hong-Yu

Abstract excerpt

Huntington's disease (HD) is an autosomally dominant neurodegenerative disorder caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein. Htt yeast two-hybrid protein B (HYPB/SETD2), a histone methyltransferase, directly interacts with Htt and is involved in HD pathology. Using NMR techniques, we characterized a polyproline (polyP) stretch at the C terminus of HYPB, which directly interacts...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Histone-Lysine N-Methyltransferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntingtin Protein

Share to Magnetic Resonance Spectroscopy

Share to Nerve Tissue Proteins

Share to Peptides

Share to Protein Conformation

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 24412394
DOI: 10.1016/j.str.2013.12.005

Genes

SETD2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin.PMID 24412394Read ↗

Huntingtin interacts with a family of WW domain proteins.Semantic proximity Read ↗

Target Recognition in Tandem WW Domains: Complex Structures for Parallel and Antiparallel Ligand Orientation in h-FBP21 Tandem WWSemantic proximity Read ↗

HAP40 orchestrates huntingtin structure for differential interaction with polyglutamine expanded exon 1Semantic proximity Read ↗

HAP40 is a conserved central regulator of Huntingtin and a specific modulator of mutant Huntingtin toxicitySemantic proximity Read ↗

Recent Advances in the Study of Huntingtin Interacting ProteinsSemantic proximity Read ↗

Structural Model of the Proline-rich Domain of Huntingtin exon-1 fibrilsSemantic proximity Read ↗

High-Affinity, Structure-Validated and Selective Macrocyclic Peptide Tools for Chemical Biology Studies of HuntingtinSemantic proximity Read ↗

The Biology of Huntingtin.Semantic proximity Read ↗

Integrative determination of the atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington’s diseaseSemantic proximity Read ↗

Macrocyclic Peptide Tools for Huntingtin-bound HAP40Semantic proximity Read ↗

New Structural Insights into Formation of the Key Actin Regulating WIP-WASp Complex Determined by NMR and Molecular Imaging.Semantic proximity Read ↗

PolyQ expansion does not alter the Huntingtin-HAP40 complexSemantic proximity Read ↗

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