ArticleProtein science : a publication of the Protein Society2004
Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 53 citations in OpenAlex.
- Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v1.0].Living journal of computational molecular science · 2025Article
- HP35 Protein in the Mesopore of MIL-101(Cr) MOF: A Model to Study Cotranslocational Unfolding.ACS omega · 2024Article
- Targeting AVIL, a New Cytoskeleton Regulator in Glioblastoma.International journal of molecular sciences · 2021Review
- F-actin-bundling sites are conserved in proteins with villin-type headpiece domains.Molecular biology of the cell · 2020Article
- Steroidal glycoalkaloids fromPeerJ · 2019Article
- Advillin acts upstream of phospholipase C ϵ1 in steroid-resistant nephrotic syndrome.The Journal of clinical investigation · 2017Article
- Drosophila Dunc-115 mediates axon projection through actin binding.Invertebrate neuroscience : IN · 2017Article
- Following easy slope paths on a free energy landscape: the case study of the Trp-cage folding mechanism.Biophysical journal · 2013Article
- Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation.Biophysical journal · 2012Article
- Competition between intradomain and interdomain interactions: a buried salt bridge is essential for villin headpiece folding and actin binding.Biochemistry · 2011Article
- Structural analysis of the conserved ubiquitin-binding motifs (UBMs) of the translesion polymerase iota in complex with ubiquitin.The Journal of biological chemistry · 2011Article
- Hydrophobic core formation and dehydration in protein folding studied by generalized-ensemble simulations.Biophysical journal · 2010Article
- Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.Journal of the American Chemical Society · 2009Article
- Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression.The FEBS journal · 2009Review
- The 3D structure of villin as an unusual F-Actin crosslinker.Structure (London, England : 1993) · 2008Article
- Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: application to the villin headpiece subdomain and the LysM domain.Biochemistry · 2008Article
- Regulation of cell structure and function by actin-binding proteins: villin's perspective.FEBS letters · 2008Review
- Evolutionary Pareto-optimization of stably folding peptides.BMC bioinformatics · 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
- Role of Drosophila gene dunc-115 in nervous system.Invertebrate neuroscience : IN · 2007Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Headpiece (HP) is a 76-residue F-actin-binding module at the C terminus of many cytoskeletal proteins. Its 35-residue C-terminal subdomain is one of the smallest known motifs capable of autonomously adopting a stable, folded structure in the absence of any disulfide bridges, metal ligands, or unnatural amino acids. We report the three-dimensional solution structures of the C-terminal headpiece subdomains of human villin (HVcHP) and human advillin (HAcHP), determined by two-dimensional 1H-NMR. They represent the second and third structures of such C-terminal headpiece subdomains to be elucidated so far. A comparison with the structure of the chicken villin C-terminal subdomain reveals a high structural conservation. Both C-terminal subdomains bind specifically to F-actin. Mutagenesis is used to demonstrate the involvement of Trp 64 in the F-actin-binding surface. The latter residue is part of a conserved structural feature, in which the surface-exposed indole ring is stacked on the proline and lysine side chain embedded in a PXWK sequence motif. On the basis of the structural and mutational data concerning Trp 64 reported here, the results of a cysteine-scanning mutagenesis study of full headpiece, and a phage display mutational study of the 69-74 fragment, we propose a modification of the model, elaborated by Vardar and coworkers, for the binding of headpiece to F-actin.
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