Molecular cloning of a novel putative potassium channel-blocking neurotoxin from the venom of the North African scorpion, Androctonus amoreuxi
Data(s) |
01/05/2005
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Identificador |
http://dx.doi.org/10.1016/j.peptides.2004.12.002 http://www.scopus.com/inward/record.url?scp=16244410163&partnerID=8YFLogxK |
Idioma(s) |
eng |
Direitos |
info:eu-repo/semantics/restrictedAccess |
Fonte |
Chen , T , Walker , B , Zhou , M & Shaw , C 2005 , ' Molecular cloning of a novel putative potassium channel-blocking neurotoxin from the venom of the North African scorpion, Androctonus amoreuxi ' Peptides , vol 26 (5) , no. 5 , pp. 731-736 . DOI: 10.1016/j.peptides.2004.12.002 |
Palavras-Chave | #/dk/atira/pure/subjectarea/asjc/1300/1303 #Biochemistry #/dk/atira/pure/subjectarea/asjc/1300/1310 #Endocrinology #/dk/atira/pure/subjectarea/asjc/1300/1314 #Physiology #/dk/atira/pure/subjectarea/asjc/2800/2804 #Cellular and Molecular Neuroscience |
Tipo |
article |
Resumo |
Scorpion venoms are a particularly rich source of neurotoxic proteins/peptides that interact in a highly specific fashion with discrete subtypes of ion channels in excitable and non-excitable cells. Here we have employed a recently developed technique to effect molecular cloning and structural characterization of a novel putative potassium channel-blocking toxin from the same sample of venom from the North African scorpion, Androctonus amoreuxi. The deduced precursor open-reading frame is composed of 59 amino acid residues that consists of a signal peptide of approximately 22 amino acid residues followed by a mature toxin of 37 amino acid residues. The mature toxin contains two functionally important residues (Lys27 and Tyr36), constituting a functional dyad motif that may be critical for potassium channel-blocking activity that can be affirmed from structural homologs as occurring in the venoms from other species of Androctonus scorpions. Parallel proteomic/transcriptomic studies can thus be performed on the same scorpion venom sample without sacrifice of the donor animal. |