Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases

FEBS Lett. 1986 Jan 6;194(2):338-42. doi: 10.1016/0014-5793(86)80113-2.

Abstract

There are 33 invariant amino acid positions out of 132 positions in 42 investigated sequences of ribonucleases from a number of mammalian species and a reptile (snapping turtle, Chelydra serpentina). These invariant residues are unequally distributed over 3 different parts of the molecule. The lobe of the S-protein part of the molecule, which lacks one disulfide bridge and has two shortened loops in turtle ribonuclease, has the lowest percentage of invariant residues, although the active-site residue His 119 is located in this part.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Endoribonucleases* / isolation & purification
  • Macromolecular Substances
  • Peptide Fragments / isolation & purification
  • Protein Conformation
  • Ribonucleases* / isolation & purification
  • Species Specificity
  • Turtles

Substances

  • Macromolecular Substances
  • Peptide Fragments
  • ribonuclease S-peptide
  • Endoribonucleases
  • Ribonucleases
  • ribonuclease SPL