ArticleProtein science : a publication of the Protein Society2011
Solution structure of the human HSPC280 protein.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 7 papers.
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7 citing papers in PubMed, 7 citations in OpenAlex.
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- The tumorigenic effect of the high expression of ABRACL in glioma and its potential as a therapeutic target.Heliyon · 2024Article
- Characterization of the Abracl-Expressing Cell Populations in the Embryonic Mammalian Telencephalon.Biomolecules · 2023Article
- Human Costars Family Protein ABRACL Modulates Actin Dynamics and Cell Migration and Associates with Tumorigenic Growth.International journal of molecular sciences · 2021Article
- miR-145-5p Inhibits the Proliferation, Migration, and Invasion of Esophageal Carcinoma Cells by Targeting ABRACL.BioMed research international · 2021Article
- HSPC280, a winged helix protein expressed in the subventricular zone of the developing ganglionic eminences, inhibits neuronal differentiation.Histochemistry and cell biology · 2016Article
- The Cardiac Stress Response Factor Ms1 Can Bind to DNA and Has a Function in the Nucleus.PloS one · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human HSPC280 protein belongs to a new family of low molecular weight proteins, which is only present in eukaryotes, and is absent in fungi. The solution structure of HSPC280 was determined using multidimensional NMR spectroscopy. The overall structure consists of three α-helices and four antiparallel β-strands and has a winged helix-like fold. However, HEPC280 is not a typical DNA-binding winged helix protein in that it lacks DNA-binding activity. Unlike most winged-helix proteins, HSPC280 has an unusually long 13-residue (P62-V74) wing 1 loop connecting the β3 and β4 strands of the protein. Molecules of HSPC280 have a positively charged surface on one side and a negatively charged surface on the other side of the protein structure. Comparisons with the C-terminal 80-residue domain of proteins in the Abra family reveal a conserved hydrophobic groove in the HSPC280 family, which may allow HSPC280 to interact with other proteins.
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