Work

Primary structure determination and cloning of the cDNA encoding toxin 4 of the scorpion Centruroides noxius Hoffmann

Year: 1993

Type: article

Abstract: A peptide (toxin II-10), shown to be a Na+ channel blocker, was purified from the venom of the scorpion Centruroides noxius Hoffmann and sequenced by Edman degradation. It has 66 amino acid residues with the C-terminal residue (asparagine) amidated, as demonstrated by mass spectrometry. In addition, we report the cloning and the nucleotide sequence of the cDNA (CngtV) that codes for this toxin. We discuss the mechanism for processing the precursor peptide to its final form and compare the primary structure to that of other Na+ channel toxins. Two distinct groups of toxins seem to emerge from this comparison, suggesting a structure-function relationship of these peptides towards the recognition of either mammalian or insect tissues.

Source: FEBS Letters

DOI: 10.1016/0014-5793(93)81654-i

Authors: A. Vázquez, B. Becerril, B.M. Martin, F. Zamudio, F. Bolívar, L.D. Possani

Institutions: Universidad Nacional Autónoma de México, National Institutes of Health, National Institute of Mental Health

Language: English

Topic: Venomous Animal Envenomation and Studies

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2024319193

FWCI: 1.685

Cites: 14

Cited by: 22

Related to: 10