ArticleProtein science : a publication of the Protein Society1994
Solution structure of villin 14T, a domain conserved among actin-severing proteins.
Article in Protein science : a publication of the Protein Society, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 52 citations in OpenAlex.
- The 3D structure of villin as an unusual F-Actin crosslinker.Structure (London, England : 1993) · 2008Article
- The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence.Biochemistry · 2007Article
- Identification of individual protein-ligand NOEs in the limit of intermediate exchange.Journal of biomolecular NMR · 2006Article
- Elucidating the mechanism of familial amyloidosis- Finnish type: NMR studies of human gelsolin domain 2.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Determination of the gelsolin binding site on F-actin: implications for severing and capping.Biophysical journal · 1998Article
- Refined structure of villin 14T and a detailed comparison with other actin-severing domains.Protein science : a publication of the Protein Society · 1997Article
- Molecular and mutational analysis of a gelsolin-family member encoded by the flightless I gene of Drosophila melanogaster.Genetics · 1995Article
- The tyrosine corner: a feature of most Greek key beta-barrel proteins.Protein science : a publication of the Protein Society · 1994Article
- 1H, 15N, 13C and 13CO resonance assignments and secondary structure of villin 14T, a domain conserved among actin-severing proteins.Journal of biomolecular NMR · 1994Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
The solution structure of the N-terminal domain of the actin-severing protein villin has been determined by multidimensional heteronuclear resonance spectroscopy. Villin is a member of a family of actin-severing proteins that regulate the organization of actin in the eukaryotic cytoskeleton. Members of this family are built from 3 or 6 homologous repeats of a structural domain of approximately 130 amino acids that is unrelated to any previously known structure. The N-terminal domain of villin (14T) contains a central beta-sheet with 4 antiparallel strands and a fifth parallel strand at one edge. This sheet is sandwiched between 2 helices on one side and a 2-stranded parallel beta-sheet with another helix on the other side. The strongly conserved sequence characteristic of the protein family corresponds to internal hydrophobic residues. Calcium titration experiments suggest that there are 2 binding sites for Ca2+, a stronger site near the N-terminal end of the longest helix, with a Kd of 1.8 +/- 0.4 mM, and a weaker site near the C-terminal end of the same helix, with a Kd of 11 +/- 2 mM. Mutational and biochemical studies of this domain in several members of the family suggest that the actin monomer binding site is near the parallel strand at the edge of the central beta-sheet.
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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.