Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint

J Mol Biol. 1986 Jan 5;187(1):101-7. doi: 10.1016/0022-2836(86)90409-2.

Abstract

An amino acid sequence "fingerprint" has been derived that can be used to test if a particular sequence will fold into a beta alpha beta-unit with ADP-binding properties. It was deduced from a careful analysis of the known three-dimensional structures of ADP-binding beta alpha beta-folds. This fingerprint is in fact a set of 11 rules describing the type of amino acid that should occur at a specific position in a peptide fragment. The total length of this fingerprint varies between 29 and 31 residues. By checking against all possible sequences in a database, it appeared that every peptide, which exactly follows this fingerprint, does indeed fold into an ADP-binding beta alpha beta-unit.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chickens
  • Dogfish
  • Glyceraldehyde-3-Phosphate Dehydrogenases / genetics
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism
  • Humans
  • L-Lactate Dehydrogenase
  • Mice
  • Mitochondrial ADP, ATP Translocases / genetics
  • Mitochondrial ADP, ATP Translocases / metabolism
  • Protein Conformation*
  • Swine

Substances

  • Mitochondrial ADP, ATP Translocases
  • L-Lactate Dehydrogenase
  • Glyceraldehyde-3-Phosphate Dehydrogenases