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

Crystal structures of the UBX domain of human UBXD7 and its complex with p97 ATPase.

Biochemical and biophysical research communications - 22 Apr 2017

Li Zhi-Hui, Wang Yong, Xu Min, Jiang Tao

Abstract excerpt

In humans, UBXD7 (also called UBXN7), an adaptor of p97 ATPase, can participate in the degradation of misfolded or damaged proteins in the p97-mediated ubiquitin proteasome system (UPS). UBXD7 binds to ubiquitinated substrates via its UBA domain and interacts with p97 N-terminal domain through its UBX domain to recruit p97 or the p97 core complex (p97/NPL4/UFD1). Here, we report the crystal structures of the UBX...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Adenosine Triphosphatases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calorimetry

Share to Crystallization

Share to Crystallography, X-Ray

Share to Disulfides

Share to Protein Domains

Share to Protein Multimerization

Source

Identifiers

PMID: 28274878
DOI: 10.1016/j.bbrc.2017.03.005

Genes

UFD1
UBXN7

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

Crystal structures of the UBX domain of human UBXD7 and its complex with p97 ATPase.PMID 28274878Read ↗

In silico prediction, Characterization, Docking studies and Molecular dynamics simulation of human p97 in complex with p37 cofactorSemantic proximity Read ↗

Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites.Semantic proximity Read ↗

Control of p97 function by cofactor binding.Semantic proximity Read ↗

Faf1 accelerates p97-mediated protein unfolding by promoting ubiquitin engagementSemantic proximity Read ↗

Interaction between the AAA+ ATPase p97 and its cofactor ataxin3 in health and disease: Nucleotide-induced conformational changes regulate cofactor binding.Semantic proximity Read ↗

Mutant p97 exhibits species-specific changes of its ATPase activity and compromises the UBXD9-mediated monomerisation of p97 hexamers.Semantic proximity Read ↗

Structure and function of the AAA+ ATPase p97/Cdc48p.Semantic proximity Read ↗

Interaction between the AAA ATPase p97/VCP and a concealed UBX domain in the copper transporter ATP7A is associated with motor neuron degeneration.Semantic proximity Read ↗

The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.Semantic proximity Read ↗

Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1.Semantic proximity Read ↗

Valosin-Containing Protein (VCP)/p97 Oligomerization.Semantic proximity Read ↗

Recent advances in p97/VCP/Cdc48 cellular functions.Semantic proximity Read ↗

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