Polypeptide chains with similar amino acid sequences but a distinctly different conformation. Bovine and porcine phospholipase A2

FEBS Lett. 1983 Nov 28;164(1):25-7. doi: 10.1016/0014-5793(83)80011-8.

Abstract

The primary structures of bovine and porcine pancreatic phospholipase A2 differ only by about 15%. Nevertheless, a 12 residue loop, with only one substitution (Val leads to Phe) has a quite different conformation, whereas the rest of the molecules have a very similar folding indeed. From this observation it is concluded that prediction of a 3-dimensional structure on the basis of sequence similarity of short segments alone might give erroneous results.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence*
  • Animals
  • Cattle
  • Models, Molecular
  • Pancreas / enzymology
  • Phospholipases A*
  • Phospholipases A2
  • Phospholipases*
  • Protein Conformation*
  • Species Specificity
  • Structure-Activity Relationship
  • Swine

Substances

  • Phospholipases
  • Phospholipases A
  • Phospholipases A2