DNA interaction and dimerization of eukaryotic SMC hinge domains.

doi:10.1074/jbc.M402439200

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

Topics Community

Back to search

Article

DNA interaction and dimerization of eukaryotic SMC hinge domains.

The Journal of biological chemistry - 18 Jun 2004

Chiu Allen, Revenkova Ekaterina, Jessberger Rolf

Abstract excerpt

The eukaryotic SMC1/SMC3 heterodimer is essential for sister chromatid cohesion and acts in DNA repair and recombination. Dimerization depends on the central hinge domain present in all SMC proteins, which is flanked at each side by extended coiled-coil regions that terminate in specific globular domains. Here we report on DNA interactions of the eukaryotic, heterodimeric SMC1/SMC3 hinge regions, using the two...

Topics

Amino Acids
Animals
Binding, Competitive
Cattle
Cell Cycle Proteins
Chromatids
Chromosomal Proteins, Non-Histone
Cloning, Molecular
DNA
DNA, Complementary
Dimerization
Dose-Response Relationship, Drug

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Glycine

Models, Biological

Models, Genetic

Mutation

Nuclear Proteins

Nucleic Acid Conformation

Source

Open in PubMed

Identifiers

PMID: 15087462
DOI: 10.1074/jbc.M402439200

Genes

SMC3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

DNA interaction and dimerization of eukaryotic SMC hinge domains.PMID 15087462Read ↗

Both interaction surfaces within cohesin's hinge domain are essential for its stable chromosomal association.Semantic proximity Read ↗

A role for the Smc3 hinge domain in the maintenance of sister chromatid cohesion.Semantic proximity Read ↗

Conserved disruptions in the predicted coiled-coil domains of eukaryotic SMC complexes: implications for structure and function.Semantic proximity Read ↗

Specialized interfaces of Smc5/6 control hinge stability and DNA association.Semantic proximity Read ↗

Cornelia de Lange syndrome mutations in SMC1A or SMC3 affect binding to DNA.Semantic proximity Read ↗

Closing the cohesin ring: structure and function of its Smc3-kleisin interface.Semantic proximity Read ↗

A cohesin cancer mutation reveals a role for the hinge domain in genome organization and gene expression.Semantic proximity Read ↗

Structure and stability of cohesin's Smc1-kleisin interaction.Semantic proximity Read ↗

SMCHD1's ubiquitin-like domain is required for N-terminal dimerization and chromatin localization.Semantic proximity Read ↗

Identification of a region in the coiled-coil domain of Smc3 that is essential for cohesin activity.Semantic proximity Read ↗

Suppressor mutation analysis combined with 3D modeling explains cohesin's capacity to hold and release DNA.Semantic proximity Read ↗

Relating SMCHD1 structure to its function in epigenetic silencing.Semantic proximity Read ↗

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