Tertiary Structural studies of Myotoxin a from Crotalus viridis viridis Venom by Nuclear Magnetic Resonance

Abstract

Myotoxin a, a 42-residue protein from the venom of the prairie rattlesnake (Crotalus viridis viridis, has been studied in aqueous solution by proton nuclear magnetic resonance (NMR) spectroscopy, and a general tertiary structure has been determined. Myotoxin a is one of a family of highly homologous myotoxins that cause localized tissue myonecrosis upon envenomation and whose structures are highly constrained by three disulfide linkages. Eighty- six relevant distance constraints derived from nuclear Overhauser enhancement spectroscopy (NOESY) experiments were employed in distance geometry calculations. A superimposed subset of the best refined structures yielded a medium resolution (backbone atoms' root mean square distance of 2.5 A) tertiary conformation. The structure consists of three strands of anti-parallel beta sheet bound by three disulfide bonds and connected by short loops and turns, including a modified type VI (cis-proline) turn.

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Document Details

Document Type
Technical Report
Publication Date
May 01, 1993
Accession Number
ADA271173

Entities

People

  • Michael P. O'keefe

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Amino Acids
  • Biochemistry
  • Cells
  • Chemical Shifts
  • Chemical Synthesis
  • Chemistry
  • Geometry
  • Liquid Chromatography
  • Magnetic Resonance
  • Membrane Potentials
  • Muscle Cells
  • Nuclear Magnetic Resonance
  • Proteins
  • Resonance
  • Skeletal Muscle
  • Three Dimensional
  • Two Dimensional

Fields of Study

  • Chemistry

Readers

  • Molecular and Cellular Biochemistry
  • Quantum spin resonance or Electron Paramagnetic Resonance spectroscopy.
  • Superconducting Magnet Technology