1orl
From Proteopedia
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1H NMR structure determination of Viscotoxin C1
Overview
The high resolution three-dimensional structure of the newly discovered, plant viscotoxin C1, from the Asiatic Viscum album ssp. Coloratum ohwi, has been determined in solution by (1)H NMR spectroscopy at pH 3.6 and 285, K. The viscotoxin C1-fold, consisting of a helix-turn-helix motif and a, short stretch of an antiparralel beta-sheet is very similar to that found, for the highly similar viscotoxins A2 and A3 and for other related, thionins. Different functional properties of members of the thionin family, are discussed here in light of the structural and electrostatic, properties. Among the very homologous family of alpha- and beta-thionins, known for their antimicrobial activity, the viscotoxin subfamily differs, from the other members because of its high toxicity against tumoral cells., Key residues for the modulation of viscotoxin cytotoxicity have been, identified on the basis of sequence and structural alignment.
About this Structure
1ORL is a Single protein structure of sequence from Viscum album. Full crystallographic information is available from OCA.
Reference
NMR solution structure of viscotoxin C1 from Viscum album species Coloratum ohwi: toward a structure-function analysis of viscotoxins., Romagnoli S, Fogolari F, Catalano M, Zetta L, Schaller G, Urech K, Giannattasio M, Ragona L, Molinari H, Biochemistry. 2003 Nov 4;42(43):12503-10. PMID:14580196
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