Localization and analysis of nonpolar regions in onconase

EY Kolbanovskaya, ACT van Scheltinga, VG Mukhortov, W Ardelt, JJ Beintema*, MY Karpeisky

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

A detailed analysis of the composition and properties of hydrophobic nuclei and microclusters has been carried out for onconase. Two main hydrophobic nuclei in the onconase structure were detected. Their composition and shape were found to be very similar to those of RNase A, in accordance with the predictions made. The nuclei in onconase are more compact, the side-chain atoms of residues included in the nuclei in onconase form more contacts with the environment than in RNase A. The hydrophobic nuclei should be considered as individual structural units along with elements of the secondary structure. Differences in composition and conformation of exposed loops between onconase and RNase A were found. The additional hydrophobic clusters attached to the nuclei in onconase might be involved in the fixation of an appropriate conformation of site(s) for manifestation of the biological activity of onconase. A comparison of amphibian representatives of the RNase A superfamily was also made. The results obtained suggest that the availability of nonpolar residues in established key positions of amino acid sequences determines the characteristic fold of homologous proteins and the structure of the active site cleft.

Original languageEnglish
Pages (from-to)1306-1316
Number of pages11
JournalCellular and molecular life sciences
Volume57
Issue number8-9
DOIs
Publication statusPublished - Aug-2000

Keywords

  • amphibians
  • hydrophobic nuclei
  • nonpolar contacts
  • onconase
  • ribonuclease A superfamily
  • AMINO-ACID-SEQUENCE
  • RANA-PIPIENS OOCYTES
  • P-30 PROTEIN
  • RIBONUCLEASE-A
  • PANCREATIC RIBONUCLEASES
  • ANTITUMOR PROTEIN
  • EARLY EMBRYOS
  • RNASE
  • CYTOTOXICITY
  • LECTIN

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