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Role of arginine residues for the activity of fasciculin
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry.
1995 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 229, no 1, 270-275 p.Article in journal (Refereed) Published
Abstract [en]

The West African green mamba, Dendroaspis angusticeps, has two toxins, fasciculins, that are non-competitive inhibitors of acetylcholinesterase. Arginine residues of fasciculin 2 were modified with 1,2-cyclohexanedione. Two of these residues, Arg24 and Arg37, reacted very slowly or not at all. Modification of Arg28 reduced the activity only by 13%. Arg11 and Arg27 are unique for fasciculins; a comparison of the sequences of 175 snake toxins homologous to fasciculins showed that no other toxin has arginine in the corresponding positions. Modification of the two unique arginines had a large effect and decreased the activity by 73% (Arg11) and 85% (Arg27). This was apparently not due to structural perturbations, since the modification did not change the circular dichroic spectra. The two arginine residues probably participate in the binding to acetylcholinesterase. They are located on the same side of the toxin molecule and the distance between their alpha-carbons is 2.7 nm. This may indicate binding to sites that are far apart and suggests that fasciculin covers a large area of the enzyme

Place, publisher, year, edition, pages
1995. Vol. 229, no 1, 270-275 p.
National Category
Natural Sciences
URN: urn:nbn:se:uu:diva-52668DOI: 10.1111/j.1432-1033.1995.0270l.xPubMedID: 7744040OAI: oai:DiVA.org:uu-52668DiVA: diva2:80578
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-07-19Bibliographically approved

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Engström, Åke
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