The spasmodic peptide defines a new conotoxin superfamily.
Grant Information: | GM48677 United States GM NIGMS NIH HHS |
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Substance Nomenclature: | 0 (Conotoxins) 0 (Conus textile toxin) 0 (Peptide Fragments) 0 (Peptides) 0 (spasmodic peptide, Conus) 53445-96-8 (1-Carboxyglutamic Acid) |
Entry Date(s): | Date Created: 20000226 Date Completed: 20000313 Latest Revision: 20190613 |
Update Code: | 20221213 |
DOI: | 10.1021/bi9923712 |
PMID: | 10677206 |
Autor: | Lirazan MB; Department of Biology, University of Utah, Salt Lake City, Utah 84112, USA., Hooper D, Corpuz GP, Ramilo CA, Bandyopadhyay P, Cruz LJ, Olivera BM |
Jazyk: | angličtina |
Zdroj: | Biochemistry [Biochemistry] 2000 Feb 22; Vol. 39 (7), pp. 1583-8. |
DOI: | 10.1021/bi9923712 |
Abstrakt: | We purified and characterized a peptide from the venom of Conus textile that makes normal mice assume the phenotype of a well-known mutant, the spasmodic mouse. This "spasmodic" peptide has 27 amino acids, including two gamma-carboxyglutamate (Gla) residues. A cDNA clone encoding the precursor for the peptide was identified; a gamma-carboxylation recognition signal sequence (gamma-CRS) is present in the -1 --> -20 region of the peptide precursor. Both the gamma-CRS and the position of the Gla residues in the mature toxin are notably different from other Gla-containing conopeptides. The spasmodic peptide has a novel disulfide framework and distinct signal sequence which together define a new P-superfamily of conopeptides. A cDNA encoding another member of the P-superfamily was identified from a different species, Conus gloriamaris. |
Databáze: | MEDLINE |
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