A particularly labile Asp-Pro bond in the green mamba muscarinic toxin MTX2. Effect of protein conformation on the rate of cleavage

The single Asp53-Pro54 bond of the MTX2 toxin from the mamba snake Dendroaspis angusticeps is rapidly and efficiently cleaved in acidic solution (pH 1.5–2.5) at 45°C. Unfolding of the toxin slows down the cleavage reaction by several times. Modelling studies indicate that the native toxin conformati...

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Veröffentlicht in:	FEBS letters 1995-09, Vol.371 (2), p.171-175
Hauptverfasser:	Ségalas, Isabelle, Thai, Robert, Claudio Vita, Renée Ménez
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical chemistry Asp-Pro bond Aspartic Acid - metabolism Biochemistry Biochemistry, Molecular Biology capillary zone electrophoresis Chemical Sciences Chromatography, High Pressure Liquid Circular Dichroism CZE Dendroaspis angusticeps muscarinic toxin 2 Elapid Venoms - chemistry Elapid Venoms - metabolism Electrophoresis Hydrogen-Ion Concentration Life Sciences Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Molecular Structure MTX2 Muscarinic toxin Neurotoxins - chemistry Neurotoxins - metabolism PE-MTX2 Peptide bond cleavage Peptide fragment Peptide Fragments - chemistry Peptide Fragments - metabolism Proline - chemistry Protein Conformation Protein degradation pyridine-ethylated MTX2 Reptilian Proteins Structural Biology Structure-Activity Relationship
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