NMR structure of the 35-residue villin headpiece subdomain
- 1 March 1997
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (3), 180-184
- https://doi.org/10.1038/nsb0397-180
Abstract
The NMR structure of an autonomously folding subdomain from villin headpiece is reported. It forms a novel three helix structure with the actin-binding residues arrayed on the C-terminal helix.Keywords
This publication has 29 references indexed in Scilit:
- A Thermostable 35-Residue Subdomain within Villin HeadpieceJournal of Molecular Biology, 1996
- Structure of Actin Binding Proteins: Insights about Function at Atomic ResolutionAnnual Review of Cell Biology, 1994
- The 100 kDa F‐actin capping protein of Dictyostelium amoebae is a villin prototype (‘protovillin’)FEBS Letters, 1993
- The High-resolution Structure of the Peripheral Subunit-binding Domain of Dihydrolipoamide Acetyltransferase from the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus stearothermophilusJournal of Molecular Biology, 1993
- In vivo analysis of functional domains from villin and gelsolin.The Journal of cell biology, 1992
- Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonanceJournal of Molecular Biology, 1988
- Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determinationJournal of Molecular Biology, 1986
- Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular proteinJournal of Molecular Biology, 1984
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Evaluation of a new broadband decoupling sequence: WALTZ-16Journal of Magnetic Resonance (1969), 1983