Localization and analysis of nonpolar regions in onconase

Citation
Ey. Kolbanovskaya et al., Localization and analysis of nonpolar regions in onconase, CELL MOL L, 57(8-9), 2000, pp. 1306-1316
Citations number
29
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420-682X → ACNP
Volume
57
Issue
8-9
Year of publication
2000
Pages
1306 - 1316
Database
ISI
SICI code
1420-682X(200008)57:8-9<1306:LAAONR>2.0.ZU;2-O
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 a toms of residues included in the nuclei in onconase form more contacts with the environment than in RNase A. The hydrophobic nuclei should be consider ed as individual structural units along with elements of the secondary stru cture. Differences in composition and conformation of exposed loops between onconase and RNase A were found. The additional hydrophobic clusters attac hed to the nuclei in onconase might be involved in the fixation of an appro priate conformation of site(s) for manifestation of the biological activity of onconase. A comparison of amphibian representatives of the RNase A supe rfamily was also made. The results obtained suggest that the availability o f nonpolar residues in established key positions of amino acid sequences de termines the characteristic fold of homologous proteins and the structure o f the active site cleft.