ArticleThe Journal of biological chemistry2002
The SCAN domain of ZNF174 is a dimer.
Article in The Journal of biological chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Epigenetic silencingCancer biology & therapy · 2024Article
- Biophysical analysis of the MHR motif in folding and domain swapping of the HIV capsid protein C-terminal domain.Biophysical journal · 2015Article
- Article
- Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206.Nucleic acids research · 2012Article
- Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- ZFP191 is required by oligodendrocytes for CNS myelination.Genes & development · 2010Article
- A decision tree model for the prediction of homodimer folding mechanism.Bioinformation · 2009Article
- A transcript profiling approach reveals the zinc finger transcription factor ZNF191 is a pleiotropic factor.BMC genomics · 2009Article
- Evolution of C2H2-zinc finger genes and subfamilies in mammals: species-specific duplication and loss of clusters, genes and effector domains.BMC evolutionary biology · 2008Article
- Structure of the SCAN domain from the tumor suppressor protein MZF1.Journal of molecular biology · 2006Article
- Structural features differentiate the mechanisms between 2S (2 state) and 3S (3 state) folding homodimers.Bioinformation · 2005Article
- Establishment of transgenic mice carrying gene encoding human zinc finger protein 191.World journal of gastroenterology · 2004Article
- Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The SCAN domain is a conserved region of 84 residues found predominantly in zinc finger DNA-binding proteins in vertebrates. The SCAN domain appears to control the association of SCAN domain containing proteins into noncovalent complexes and may be the primary mechanism underlying partner choice in the oligomerization of these transcription factors. Here we have overexpressed, purified, and characterized the isolated SCAN domain (amino acids 37-132) from ZNF174. Both size exclusion chromatography and equilibrium sedimentation analysis demonstrate that the ZNF174 SCAN domain forms a homodimer. Circular dichroism shows that the isolated SCAN domain dimer has approximately 42% alpha-helix. Thermal denaturation experiments indicate that the SCAN domain undergoes a single reversible unfolding transition with a T(m) of over 70 degrees C. The midpoint of the equilibrium unfolding transition increases with increasing protein concentration, consistent with a two-state unfolding transition in which folded dimer is in equilibrium with unfolded monomer. These findings demonstrate that the isolated SCAN domain forms a stable dimer and support a model in which the SCAN domain is capable of mediating the selective dimerization of a large family of vertebrate-specific, zinc finger-containing transcription factors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.