PMID: 8953220Oct 1, 1996Paper

The secondary structure of a pyrimidine-guanine sequence-specific ribonuclease possessing cytotoxic activity from the oocytes of Rana catesbeiana

Journal of Biomolecular NMR
C ChenT Huang

Abstract

RC-RNase is a pyrimidine-guanine sequence-specific ribonuclease and a sialic-acid-binding lectin purified from Rana catesbeiana (bullfrog) oocytes. This 111-amino acid protein exhibits cytotoxicity toward several tumor cell lines. In this paper we report the assignments of proton NMR resonances and the identification of the secondary structure deduced from NOE constraints, chemical shift index, 3JNH alpha and amide proton exchange rates. The protein was directly isolated from bullfrog oocytes; we were able to assign all but five of the amino acid backbone protons of the unlabeled protein by analyzing a large set of two-dimensional proton NMR spectra obtained at several temperatures and pH conditions. Our results indicate that the structure of RC-RNase is dominated by the presence of two triple-stranded antiparallel beta-sheets and three alpha-helices, similar to those of the pyrimidine family ribonucleases. Two sets of resonances were observed for 11 amide protons and 8 alpha-protons located in the loop-1 region, an alpha 2 helix, and three beta-strands, (beta 1, beta 3 and beta 4), suggesting the presence of nonlocalized multiple conformations for RC-RNase.

References

Nov 1, 1992·Journal of Biomolecular NMR·M PiottoV Sklenár
Nov 20, 1991·Journal of Molecular Biology·D S WishartF M Richards
Nov 1, 1989·Journal of Biochemistry·R NittaM Irie
Dec 16, 1983·Biochemical and Biophysical Research Communications·M RanceK Wüthrich
Sep 15, 1994·European Journal of Biochemistry·C ReisdorfG Spik
Jun 21, 1994·Proceedings of the National Academy of Sciences of the United States of America·R J YouleM Gravell

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Citations

Aug 25, 2015·Archives of Biochemistry and Biophysics·Chun-Hua HsuChinpan Chen
Dec 3, 2003·The Journal of Biological Chemistry·Vitaliy Y GorbatyukTai-huang Huang

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