A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2018; you can also visit the original URL.
The file type is
DNA Binding Provides a Molecular Strap Activating the Adenovirus Proteinase
Molecular & Cellular Proteomics
Human adenovirus proteinase (AVP) requires two cofactors for maximal activity: pVIc, a peptide derived from the C terminus of adenovirus precursor protein pVI, and the viral DNA. Synchrotron protein footprinting was used to map the solvent accessible cofactor binding sites and to identify conformational changes associated with the binding of cofactors to AVP. The binding of pVIc alone or pVIc and DNA together to AVP triggered significant conformational changes adjacent to the active site cleftdoi:10.1074/mcp.m400037-mcp200 pmid:15220401 fatcat:jsuhpaf4gjhefemgvmdiiw67tm