Search results for: Josep Ubach
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Synaptotagmin 1 probably functions as a Ca2+ sensor in neurotransmitter release via its two C2-domains, but no common Ca2+-dependent activity that could underlie a cooperative action between them has been described. The NMR structure of the C2B-domain now reveals a β sandwich that exhibits striking similarities and differences with the C2A-domain. Whereas the bottom face of the C2B-domain has two...
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Syntaxin 1A plays a central role in neurotransmitter release through multiple protein–protein interactions. We have used NMR spectroscopy to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure. This 120-residue N-terminal domain is conserved in plasma membrane syntaxins but not in other syntaxins, indicating a specific role in exocytosis...
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The 15-residue hybrid peptide containing residues 1-7 from cecropin A and residues 2-9 from melittin, CA(1-7)M(2-9), is a potent antibiotic with broader activity than cecropin A but without the cytotoxic character of melittin. In the presence of the helix inducer hexafluoroisopropanol the peptide forms aggregates of amphipathic α-helices. Aggregation causes very slow proton-deuterium exchange in...
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FEBS Letters > 1992 > 296 > 2 > 190-194
We have earlier reported two 26-residue antibacterial peptides made up from different segments ol'cecropin A (CA) and melittin (M). We now report a substantial reduction in size at the C-terminal section of the highly active hybrid CA(1-8)M(1-18), leading to a series of 20-, 18- and 15-residue analogs with antibiotic properties similar to the larger molecule. In particular, the 15-residue hybrids...
