Proline brackets and identification of potential functional sites in proteins: Toxins to therapeutics

Toxicon

Volumn 36, Issue 11, 1998, Pages 1659-1670

  Kini, R Manjunatha ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; PROLINE; TOXIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; CONFERENCE PAPER; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; RAT; STRUCTURE ACTIVITY RELATION; TOXIN STRUCTURE;

EID: 0031740746     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(98)00159-7     Document Type: Conference Paper

References (34)

1. Albrand J. P., Blackledge M. J., Pascaud F., Hollecker M., Marion D. NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom. Biochemistry. 34:1995;5923-5937.
2. Brown L. R., Wuthrich K. Nuclear magnetic resonance solution structure of the α-neurotoxin from the black mamba (Dendroaspis polylepis polylepis). J. Mol. Biol. 227:1992;1118-1135.
3. Cierniewski C. S., Budzynski A. Z. Involvement of the α chain in fibrin clot formation. Effect of monoclonal antibodies. Biochemistry. 31:1992;4248-4253.
4. Cserzo M., Simon I. Regularities in the primary structure of proteins. Int. J. Peptide Protein Res. 34:1989;184-195.
5. DeWielle J. R., Schweitz H., Maes P., Tartar A., Lazdunski M. Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channel. Proc. Natl. Acad. Sci. U.S.A. 88:1991;2437-2440.
6. Hatanaka H., Oka M., Kohda D., Tate S., Suda A., Tamiya N., Inagaki F. Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance. J. Mol. Biol. 240:1994;155-166.
7. 3) antagonist with a neurotoxin fold Eur. J. Biochem. 226:1994;861-868.
8. Joubert F. J., Taljaard N. The complete primary structure of toxin C from Dendroaspis polylepis polylepis (black mamba) venom. S. Afr. J. Chem. 31:1978;107-110.
9. 10) from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom. Biochim. Biophys. Acta. 579:1979;228-233.
10. Joubert F. J., Taljaard N. The complete primary structures of two reduced and S-carboxymethylated angusticeps-type toxins from Dendroaspis angusticeps. Biochim. Biophys. Acta. 623:1980;449-456.
11. 8) from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom. Int. J. Biochem. 12:1980;567-574.
12. 2. J. Biol. Chem. 262:1987;14.402-14.407.
13. Kini, R. M. and Evans, H. J. (1994) A common structural feature enclosing interaction sites: Prediction of protein-protein interaction sites and development of potent bioactive peptides. In Current Topics in Peptide and Protein Research, ed. J. Menon, Vol. 1, pp. 297-311, Council of Scientific Information, Trivandrum.
14. Kini R. M., Evans H. J. A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites. Biochem. Biophys. Res. Commun. 212:1995;1115-1124.
15. Kini R. M., Evans H. J. A novel approach to the design of potent bioactive peptides by incorporation of proline brackets: Antiplatelet effects of Arg-Gly-Asp peptides. FEBS Lett. 375:1995;15-17.
16. Kini R. M., Evans H. J. Prediction of potential protein-protein interaction sites from amino acid sequence. Identification of a fibrin polymerization site. FEBS Lett. 385:1996;81-86.
17. 1H -nuclear-magnetic-resonance assignments Eur. J. Biochem. 177:1988;295-305.
18. Le Du M. H., Marchot P., Bougis P. E., Fontecilla-Camps J. C. 1.9 Å resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba venom. J. Biol. Chem. 267:1992;22122-22130.
19. McDowell R. S., Dennis M. S., Louie A., Shuster M., Mulkerrin M. G., Lazarus R. A. Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins. Biochemistry. 31:1992;4766-4772.
20. Mebs, D. and Claus, I. (1991) Appendix. Amino acid sequences and toxicities of snake venom components. In Snake Toxins, ed. A. L. Harvey, pp. 425-447, Pergamon Press, New York.
21. Menegatti E., Tedeschi G., Ronchi S., Bortolotti F., Ascenzi P., Thomas R. N., Bolognesi M., Palmieri S. Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white mustard (Sinapis alba L.) seed. FEBS Lett. 301:1992;10-14.
22. Menez A. Les structures des toxines des animaux venimeux. Pour la Science. 190:1993;34-40.
23. Menez A., Dauplais M. As deadly as a scorpion's sting. The diversity of toxins in scorpion venoms. Sci. Spectra. 8:1997;44-50.
24. Menez A., Bontems F., Roumestand C., Gilquin B., Toma F. Structural basis for functional diversity of animal toxins. Proc. Royal Soc. Edin. 99B:1993;83-103.
25. Pillet L., Tremeau O., Ducancel F., Drevet P., Zinn-Justin S., Pinkasfeld S., Boulain J. C., Menez A. Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis. J. Biol. Chem. 268:1993;909-916.
26. Robinson A. B., Robinson L. R. Distribution of glutamine and asparagine residues and their near neighbors in peptides and proteins. Proc. Natl. Acad. Sci. U.S.A. 88:1991;8880-8884.
27. Strydom D. J. Snake venom toxins: The amino acid sequences of two toxins from Dendroaspis polylepis polylepis (black mamba) venom. J. Biol. Chem. 247:1972;4029-4042.
28. Strydom D. J. Snake venom toxins: The amino acid sequences of two toxins from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom. Biochim. Biophys. Acta. 328:1973;491-509.
29. Strydom D. J. Snake venom toxins: The amino acid sequence of a short-neurotoxin homologue from Dendroaspis polylepis polylepis (black mamba) venom. Eur. J. Biochem. 76:1977;99-106.
30. Tremeau O., Lemaire C., Drevet P., Pinkasfeld S., Ducancel F., Boulain J. C., Menez A. Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis. J. Biol. Chem. 270:1995;9362-9369.
31. VII from Dendroaspis angusticeps venom. J. Biol. Chem. 248:1973;4915-4919.
32. Watanabe T. X., Itahara Y., Kuroda H., Chen Y. N., Kimura T., Sakakibara S. Smooth muscle relaxing and hypotensive activities of synthetic calciseptine and the homologous snake venom peptide FS2. Jpn. J. Pharmacol. 68:1995;305-313.
33. Williams, J. A., Lu, X., Rahman, S., Keeting, C. and Kakkar, V. (1993) Dendroaspin: A potent integrin receptor inhibitor from the venoms of Dendroaspis viridis and D. jamesonii. Biochem. Soc. Trans. 21, 735.
34. Yao J., Feher V. A., Espejo B. F., Reymond M. T., Wright P. E., Dyson H. J. Stabilization of a type VI turn in a family of linear peptides in water solution. J. Mol. Biol. 243:1994;736-753.