Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif

Journal of Molecular Biology

Volumn 294, Issue 5, 1999, Pages 1327-1336

  Craik, David J ^a   Daly, Norelle L ^a   Bond, Trudy ^a   Waine, Clement ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Cyclic peptides; Cyclotides; Cystine knot; Kalata B1; NMR spectroscopy

Indexed keywords

CYCLOPEPTIDE; CYSTINE; PLANT EXTRACT;

ARTICLE; BETA SHEET; DISULFIDE BOND; HIGHER PLANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RUBIACEAE; SEQUENCE HOMOLOGY;

OLDENLANDIA AFFINIS; VIOLA HEDERACEAE; VIOLA ODORATA;

EID: 0033579483     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3383     Document Type: Article

References (30)

1. Benham C. J., Jafri M. S. Disulfide bonding patterns and protein topologies. Protein Sci. 2:1993;41-54.
2. Broekaert W. F., Terras F. R. G., Cammue B. P. A., Osborn R. W. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol. 108:1995;1353-1358.
3. Claeson P., Göransson U., Johansson S., Luijendijk T., Bohlin L. Fractionation protocol for the isolation of polypeptides from plant biomass. J. Nat. Prod. 61:1998;77-81.
4. Daly N. L., Koltay A., Gustafson K. R., Boyd M. R., Casas-Finet J. R., Craik D. J. Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity. J. Mol. Biol. 285:1999a;333-345.
5. Daly N. L., Love S., Alewood P. F., Craik D. J. Chemical synthesis and folding of large cyclic polypeptides: studies of the cystine knot polypeptide kalata B1. Biochemistry. 38:1999b;10606-10614.
6. De Young L. R., Burton L. E., Liu J., Powell M. F., Schmelzer C. H., Skelton N. J. RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism. Protein Sci. 5:1996;1554-1566.
7. Evans T. C. Jr., Benner J., Xu M. Q. The cyclization and polymerization of bacterially expressed proteins using modified self-splicing inteins. J. Biol. Chem. 274:1999;18359-18363.
8. Favel A., Mattras H., Coletti-Previero M. A., Zwilling R., Robinson E. A., Castro B. Protease inhibitors from Ecballium elaterium seeds. Int. J. Pept. Protein Res. 33:1989;202-208.
9. Göransson U., Luijendijk T., Johansson S., Bohlin L., Claeson P. Seven novel macrocyclic polypeptides from Viola arvensis. J. Nat. Prod. 62:1999;283-286.
10. Gran L. An oxytocic principle found in Oldenlandia affinis DC. Medd. Nor. Farm. Selsk. 12:1970;173-180.
11. Gran L. Isolation of oxytocic peptides from Oldenlandia affinis by solvent extraction of tetraphenylborate complexes and chromatography on sephadex LH-20. Lloydia. 36:1973;207-208.
12. Gustafson K. R., Sowder R. C. II, Henderson L. E., Parsons I. C., Kashman Y., Cardellina J. H. II, McMahon J. B., Buckheit R. W. Jr, Pannell L. K., Boyd M. R. Circulins A and B: novel HIV-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia. J. Am. Chem. Soc. 116:1994;9337-9338.
13. Isaacs N. W. Cystine knots. Curr. Opin. Struct. Biol. 5:1995;391-395.
14. Laskowski R. A., Rullmannn J. A., MacArthur M. W., Kaptein R., Thornton J. M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;477-486.
15. Mansfield M. L. Are there knots in proteins? Struct. Biol. 1:1994;213-214.
16. Mao B. Topological chirality of proteins. Protein Sci. 2:1993;1057-1059.
17. McDonald N. Q., Hendrickson W. A. A structural superfamily of growth factors containing a cystine knot motif. Cell. 73:1993;421-424.
18. Mislow K., Liang C. Knotted structures in chemistry, biochemistry and molecular biology. Croatica Chemica Acta. 69:1996;1385-1403.
19. Murray-Rust J., McDonald N. Q., Blundell T. L., Hosang M., Oefner C., Winkler F., Bradshaw R. A. Topological similarities in TGF-β2, PDGF-BB and NGF define a superfamily of polypeptide growth factors. Structure. 1:1993;153-159.
20. Narasimhan L., Singh J., Humblet C., Guruprasad K., Blundell T. Snail and spider toxins share a similar tertiary structure and 'cystine motif'. Struct. Biol. 1:1994;850-852.
21. Nielsen K. J., Thomas L., Lewis R. J., Alewood P. F., Craik D. J. A consensus structure for omega-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202. J. Mol. Biol. 263:1996;297-310.
22. Norton R. S., Pallaghy P. K. The cystine knot structure of ion channel toxins and related polypeptides. Toxicon. 36:1998;573-583.
23. Pallaghy P. K., Nielsen K. J., Craik D. J., Norton R. S. A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci. 3:1994;1833-1839.
24. Saether O., Craik D. J., Campbell I. D., Sletten K., Juul J., Norman D. G. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry. 34:1995;4147-4158.
25. Schöpke T., Hasan Agha M. I., Kraft R., Otto A., Hiller K. Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray. Sci. Pharm. 61:1993;145-153.
26. Takusagawa F., Kamitori S. A real knot in protein. J. Am. Chem. Soc. 118:1996;8945-8946.
27. Tam J. P., Lu Y.-A., Yu Q. Thia zip reaction for synthesis of large cyclic peptides: mechanisms and applications. J. Am. Chem. Soc. 121:1999a;4316-4324.
28. Tam J. P., Lu Y. A., Yang J. L., Chiu K. W. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc. Natl Acad. Sci. USA. 96:1999b;8913-8118.
29. Vervoot J., van den Hooven H. W., Berg A., Vossen P., Vogelsang R., Joosten M. H. A. J., de Wit P. J. G. M. The race-specific elicitor AVR9 of the tomato pathogen Cladosporium fulvum: a cystine knot protein. FEBS Letters. 404:1997;153-158.
30. Witherup K. M., Bogusky M. J., Anderson P. S., Ramjit H., Ransom R. W., Wood T., Sardana M. Cyclopsychotride A, A biologically active, 31-residue cyclic peptide isolated from Psychotria Longipes. J. Nat. Prod. 57:1994;1619-1625.