Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Crosslinking of and coupling to viral capsid proteins by tyrosine oxidation

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

related to degree

  • Strable, Erica, Ph.D. in Biochemistry, Scripps Research 2000 - 2006

authors

  • Meunier, S.
  • Strable, Erica
  • Finn, M.G.

publication date

  • March 2004

journal

  • Chemistry & Biology  Journal

abstract

  • Cowpea mosaic virus is composed of 60 identical copies of a two-subunit protein organized in pentameric assemblies around the icosahedral 5-fold symmetry axis. Treatment of the virus with the Ni(II) complex of the tripeptide GGH and a peroxide oxidant, or irradiation in the presence of Ru(bpy)(3)(2+) and persulfate generates covalent crosslinks across the pentameric subunit boundaries, effectively stitching the subunits together. Intersubunit crosslinking was found to occur exclusively at adjacent tyrosine residues (Y52-Y103), as predicted from the X-ray crystal structure of the capsid, and to be more extensive with the photochemical ruthenium system. The Ni/GGH oxidative procedure was also used to make covalent attachments to the virion by trapping with a functionalized disulfide reagent.

subject areas

  • Capsid Proteins
  • Comovirus
  • Cross-Linking Reagents
  • Crystallography, X-Ray
  • Cysteine
  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Molecular Structure
  • Mutation
  • Nickel
  • Oxidation-Reduction
  • Peptides
  • Photochemistry
  • Phthalic Acids
  • Protein Structure, Quaternary
  • Ruthenium
  • Spectrum Analysis
  • Temperature
  • Tyrosine
  • Virion
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 1074-5521

Digital Object Identifier (DOI)

  • 10.1016/j.chembiol.2004.02.019

PubMed ID

  • 15123261
scroll to property group menus

Additional Document Info

start page

  • 319

end page

  • 326

volume

  • 11

issue

  • 3

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support