Comparative protein modeling by satisfaction of spatial restraints

Mol Med Today. 1995 Sep;1(6):270-7. doi: 10.1016/s1357-4310(95)91170-7.

Abstract

Approximately one third of known protein sequences are related to at least one known protein structure. As a result, an order of magnitude more sequences can be modeled by comparative modeling than there are experimentally determined protein structures. A large fraction of these models has an accuracy approaching that of a low resolution X-ray structure or a medium resolution nuclear magnetic resonance structure. The number of applications where homology modeling has been proven useful is growing rapidly.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chymases
  • Computer Simulation
  • Crystallography, X-Ray
  • Mice
  • Models, Molecular*
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation*
  • Proteins / chemistry*
  • Serine Endopeptidases / chemistry
  • Software
  • Tryptases

Substances

  • Proteins
  • Tpsb2 protein, mouse
  • Serine Endopeptidases
  • chymase 2
  • Chymases
  • Tpsab1 protein, mouse
  • Tryptases