ArticleProtein science : a publication of the Protein Society1997
Refined structure of villin 14T and a detailed comparison with other actin-severing domains.
Article in Protein science : a publication of the Protein Society, 1997. 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, 31 citations in OpenAlex.
- An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.Journal of biomolecular structure & dynamics · 2013Article
- Discrete molecular dynamics: an efficient and versatile simulation method for fine protein characterization.The journal of physical chemistry. B · 2012Article
- Helix straightening as an activation mechanism in the gelsolin superfamily of actin regulatory proteins.The Journal of biological chemistry · 2009Article
- 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
- Structural analysis of an Echinococcus granulosus actin-fragmenting protein by small-angle x-ray scattering studies and molecular modeling.Biophysical journal · 2006Article
- Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization.The Plant cell · 2005Article
- 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
- Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis.Plant physiology · 2000Article
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3 authors at 2 institutions in 1 country.
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Abstract
Villin 14T is the amino terminal actin monomer binding domain from the actin-severing and bundling protein villin. Its structure has been determined in solution using heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopy (Markus MA, Nakayama T, Matsudaira P, Wagner G. 1994. Solution structure of villin 14T, a domain conserved among actin-severing proteins. Protein Science 3:70-81). An additional nuclear Overhauser effect (NOE) spectroscopy data set, acquired using improved gradient techniques, and further detailed analysis of existing data sets, produced an additional 601 NOE restraints for structure calculations. The overall fold does not change significantly with the additional NOE restraints but the definition of the structure is improved, as judged by smaller deviations among an ensemble of calculated structures that adequately satisfy the NMR restraints. Some of the side chains, especially those in the hydrophobic core of the domain, are much more defined. This improvement in the detail of the solution structure of villin 14T makes it interesting to compare the structure with the crystal structure of gelsolin segment 1, which shares 58% sequence identity with villin 14T, in an effort to gain insight into villin 14T's weaker affinity for actin monomers. Villin 14T has smaller side chains at several positions that make hydrophobic contacts with actin in the context of gelsolin segment 1. The structure is also compared with the structure of the related actin-severing domain, severin domain 2.
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