Structural Characterisation of the E. coli Heat Stable Enterotoxin STh

Matecko I, Burmann BM, Schweimer K, Kalbacher H, Einsiedel J, Gmeiner P, Rösch P (2008)

Publication Language: English

Publication Type: Journal article

Publication year: 2008

Journal

Open Spectroscopy Journal Bentham open

Book Volume: 2

Pages Range: 34-39

DOI: 10.2174/1874383800802010034

Abstract

E. coli heat stable enterotoxin STa is an agonist of the membrane guanylate cyclase C whose endogenous ligands are the peptide hormones guanylin and uroguanylin. Whereas these peptides contain only two disulfide bonds, STa is stabilized by one additional disulfide bridge. We chemically synthesized the enterotoxin STh that originates from the E. coli strain found in humans, and we determined its structure and its dynamics by nuclear magnetic resonance spectroscopy and molecular dynamics calculations. Chemical synthesis clearly proved successful and resulted in the formation of the native disulfide bonds. The endogenous ligands guanylin and uroguanylin show the same general structural features and dynamics properties as the enterotoxin.

Authors with CRIS profile

Jürgen Einsiedel Lehrstuhl für Pharmazeutische Chemie Peter Gmeiner Lehrstuhl für Pharmazeutische Chemie

Involved external institutions

Universität Bayreuth DE Germany (DE) Eberhard Karls Universität Tübingen DE Germany (DE)

How to cite

APA:

Matecko, I., Burmann, B.M., Schweimer, K., Kalbacher, H., Einsiedel, J., Gmeiner, P., & Rösch, P. (2008). Structural Characterisation of the E. coli Heat Stable Enterotoxin STh. Open Spectroscopy Journal, 2, 34-39. https://doi.org/10.2174/1874383800802010034

MLA:

Matecko, Irena, et al. "Structural Characterisation of the E. coli Heat Stable Enterotoxin STh." Open Spectroscopy Journal 2 (2008): 34-39.

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