Protein structure alignment

J Mol Biol. 1989 Jul 5;208(1):1-22. doi: 10.1016/0022-2836(89)90084-3.

Abstract

A new method of comparing protein structures is described, based on distance plot analysis. It is relatively insensitive to insertions and deletions in sequence and is tolerant of the displacement of equivalent substructures between the two molecules being compared. When presented with the co-ordinate sets of two structures, the method will produce automatically an alignment of their sequences based on structural criteria. The method uses the dynamic programming optimization technique, which is widely used in the comparison of protein sequences and thus unifies the techniques of protein structure and sequence comparison. Typical structure comparison problems were examined and the results of the new method compared to the published results obtained using conventional methods. In most examples, the new method produced a result that was equivalent, and in some cases superior, to those reported in the literature.

MeSH terms

  • Algorithms
  • Amino Acids
  • Animals
  • Azurin
  • Calcium-Binding Proteins
  • Hemoglobins
  • Mathematics
  • Models, Molecular
  • Muramidase
  • Myoglobin
  • Plastocyanin
  • Protein Conformation
  • Proteins*
  • Thiosulfate Sulfurtransferase

Substances

  • Amino Acids
  • Calcium-Binding Proteins
  • Hemoglobins
  • Myoglobin
  • Proteins
  • Azurin
  • Plastocyanin
  • Thiosulfate Sulfurtransferase
  • Muramidase