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Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain

By Gretchen Meinke, Paul Phelan, Amélie Fradet-Turcotte, Jacques Archambault and Peter A. Bullock

Abstract

With the aim of forming the ‘lock-washer’ conformation of the origin-binding domain of SV40 large T antigen in solution, using structure-based analysis an intermolecular disulfide bridge was engineered into the origin-binding domain to generate higher order oligomers in solution. The 1.7 Å resolution structure shows that the mutant forms a spiral in the crystal and has the de novo disulfide bond at the protein interface, although structural rearrangements at the interface are observed relative to the wild type

Topics: Research Papers
Publisher: International Union of Crystallography
OAI identifier: oai:pubmedcentral.nih.gov:3107053
Provided by: PubMed Central

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Citations

  1. (2011). SV40 large T antigen DNA-binding domain Acta Cryst.