Refinement of the solution structure of the heparin-binding domain of vascular endothelial growth factor using residual dipolar couplings

J Biomol NMR. 2002 May;23(1):57-61. doi: 10.1023/a:1015346504499.

Abstract

Previous NMR structural studies of the heparin-binding domain of vascular endothelial growth factor (VEGF165) revealed a novel fold comprising two subdomains, each containing two disulfide bridges and a short two-stranded antiparallel beta-sheet. The mutual orientation of the two subdomains was poorly defined by the NMR data. Heteronuclear relaxation data suggested that this disorder resulted from a relative lack of experimental restraints due to the limited size of the interface, rather than inherent high-frequency flexibility. Refinement of the structure using 1H(N-15N residual dipolar coupling restraints results in significantly improved definition of the relative subdomain orientations.

MeSH terms

  • Binding Sites
  • Endothelial Growth Factors / chemistry*
  • Endothelial Growth Factors / metabolism
  • Heparin / metabolism*
  • Intercellular Signaling Peptides and Proteins / chemistry*
  • Intercellular Signaling Peptides and Proteins / metabolism
  • Lymphokines / chemistry*
  • Lymphokines / metabolism
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary*
  • Vascular Endothelial Growth Factor A
  • Vascular Endothelial Growth Factors

Substances

  • Endothelial Growth Factors
  • Intercellular Signaling Peptides and Proteins
  • Lymphokines
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • Vascular Endothelial Growth Factors
  • Heparin

Associated data

  • PDB/1KMX