Crystal Structure of the Oligomerization Domain of NSP4 from Rotavirus Reveals a Core Metal-binding Site
- 1 December 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 304 (5) , 861-871
- https://doi.org/10.1006/jmbi.2000.4250
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (GM08309, GM44038)
This publication has 43 references indexed in Scilit:
- Effects of side-chain characteristics on stability and oligomerization state of a de Novo -designed model coiled-coil: 20 amino acid substitutions in position “d” 1 1Edited by P. E. WrightJournal of Molecular Biology, 2000
- De novo design of a model peptide sequence to examine the effects of single amino acid substitutions in the hydrophobic core on both stability and oligomerization state of coiled-coilsJournal of Molecular Biology, 1999
- Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residuesJournal of Molecular Biology, 1998
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Age-Dependent Diarrhea Induced by a Rotaviral Nonstructural GlycoproteinScience, 1996
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996
- Rotavirus vaccines: success by reassortment?Science, 1994
- Structure of influenza haemagglutinin at the pH of membrane fusionNature, 1994
- Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron RadiationScience, 1991
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991