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Titolo:
FLANKING PROLINE RESIDUES IDENTIFY THE L-TYPE CA2-SITE OF CALCISEPTINE AND FS2( CHANNEL BINDING)
Autore:
KINI RM; CALDWELL RA; WU QY; BAUMGARTEN CM; FEHER JJ; EVANS HJ;
Indirizzi:
NATL UNIV SINGAPORE,FAC SCI,BIOSCI CTR SINGAPORE 119260 SINGAPORE VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT BIOCHEM & MOL BIOPHYS RICHMOND VA 23298 VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT PHYSIOL RICHMOND VA23298
Titolo Testata:
Biochemistry
fascicolo: 25, volume: 37, anno: 1998,
pagine: 9058 - 9063
SICI:
0006-2960(1998)37:25<9058:FPRITL>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; BLACK MAMBA VENOM; DENDROASPIS-POLYLEPIS-POLYLEPIS; NUCLEAR-MAGNETIC-RESONANCE; PROTEIN INTERACTION SITES; SNAKE-VENOM; CALCIUM-CHANNEL; DIRECTED MUTAGENESIS; SECONDARY STRUCTURE; ALPHA-NEUROTOXIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
R.M. Kini et al., "FLANKING PROLINE RESIDUES IDENTIFY THE L-TYPE CA2-SITE OF CALCISEPTINE AND FS2( CHANNEL BINDING)", Biochemistry, 37(25), 1998, pp. 9058-9063

Abstract

Calciseptine and FS2 are 60-amino acid polypeptides, isolated from venom of the black mamba (Dendroaspis polylepis polylepis), that block voltage-dependent L-type Ca2+ channels. We predicted that these polypeptides contain an identical functional site between residues 43 and 46 by searching for proline residues that mark the flanks of protein-protein interaction sites [Kini, R. M., and Evans, H. J. (1966) FEBS Lett.385, 81-86], The predicted Ca2+ channel binding site also occurs in closely related toxins, C10S2C2 and S4C8 Therefore, it is likely that these toxins also will block L-type Ca2+ channels. To test the proposedbinding site on calciseptine and FS2, an eight-residue peptide, namedL-calchin (L-type calcium channel inhibitor), was synthesized and examined for biological activity. As expected for an L-type Ca2+ channel blocker, L-calchin reduced peak systolic and developed pressure in isolated rat heart Langendorff preparations without affecting diastolic pressure or heart rate. Furthermore, L-calchin caused a voltage-independent block of L-type Ca2+ channel currents in whole-cell patch-clampedrabbit ventricular myocytes. Thus the synthetic peptide exhibits the L-type Ca2+ channel blocking properties of the parent molecules, calciseptine and FS2, but with a lower potency. These results strongly support the identification of a site in calciseptine and FS2 that is important for binding to L-type Ca2+ channels and reinforce the importance of proline brackets flanking protein-protein interaction sites.

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Documento generato il 24/09/20 alle ore 21:32:27