메뉴 건너뛰기




Volumn 357, Issue 5, 2006, Pages 1522-1535

Discovery and characterization of a linear cyclotide from Viola odorata: Implications for the processing of circular proteins

Author keywords

Circular peptides; Cyclic cystine knot; Cyclotides; Viola odorata; Violacin A

Indexed keywords

CYCLOTIDE; PEPTIDE DERIVATIVE; PLANT EXTRACT; UNCLASSIFIED DRUG; VIOLACIN A;

EID: 33645047649     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.01.051     Document Type: Article
Times cited : (92)

References (43)
  • 1
    • 0033579483 scopus 로고    scopus 로고
    • Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
    • D.J. Craik, N.L. Daly, T. Bond, and C. Waine Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif J. Mol. Biol. 294 1999 1327 1336
    • (1999) J. Mol. Biol. , vol.294 , pp. 1327-1336
    • Craik, D.J.1    Daly, N.L.2    Bond, T.3    Waine, C.4
  • 2
    • 14844315799 scopus 로고    scopus 로고
    • Oxidative folding of the cystine knot motif in cyclotide proteins
    • D.J. Craik, and N.L. Daly Oxidative folding of the cystine knot motif in cyclotide proteins Protein Pept. Letters 12 2005 147 152
    • (2005) Protein Pept. Letters , vol.12 , pp. 147-152
    • Craik, D.J.1    Daly, N.L.2
  • 3
    • 0036489968 scopus 로고    scopus 로고
    • The cyclotides: Novel macrocyclic peptides as scaffolds in drug design
    • D.J. Craik, S. Simonsen, and N.L. Daly The cyclotides: novel macrocyclic peptides as scaffolds in drug design Curr. Opin. Drug Discov. Dev. 5 2002 251 260
    • (2002) Curr. Opin. Drug Discov. Dev. , vol.5 , pp. 251-260
    • Craik, D.J.1    Simonsen, S.2    Daly, N.L.3
  • 4
    • 4444359659 scopus 로고    scopus 로고
    • Novel strategies for isolation and characterization of cyclotides: The discovery of bioactive macrocyclic plant polypeptides in the Violaceae
    • U. Göransson, E. Svangard, P. Claeson, and L. Bohlin Novel strategies for isolation and characterization of cyclotides: the discovery of bioactive macrocyclic plant polypeptides in the Violaceae Curr. Protein Pept. Sci. 5 2004 317 329
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 317-329
    • Göransson, U.1    Svangard, E.2    Claeson, P.3    Bohlin, L.4
  • 7
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • D.J. Craik, N.L. Daly, and C. Waine The cystine knot motif in toxins and implications for drug design Toxicon 39 2001 43 60
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 8
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • P.K. Pallaghy, K.J. Nielsen, D.J. Craik, and R.S. Norton 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
    • (1994) Protein Sci. , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 9
    • 0033534366 scopus 로고    scopus 로고
    • Solution structure by NMR of circulin A: A macrocyclic knotted peptide having anti-HIV activity
    • N.L. Daly, A. Koltay, K.R. Gustafson, M.R. Boyd, J.R. Casas-Finet, and D.J. Craik Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity J. Mol. Biol. 285 1999 333 345
    • (1999) J. Mol. Biol. , vol.285 , pp. 333-345
    • Daly, N.L.1    Koltay, A.2    Gustafson, K.R.3    Boyd, M.R.4    Casas-Finet, J.R.5    Craik, D.J.6
  • 10
    • 0036495674 scopus 로고    scopus 로고
    • Circular proteins - No end in sight
    • M. Trabi, and D.J. Craik Circular proteins - no end in sight Trends Biochem. Sci. 27 2002 132 138
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 132-138
    • Trabi, M.1    Craik, D.J.2
  • 11
    • 0034793341 scopus 로고    scopus 로고
    • Plant cyclotides: Circular, knotted peptide toxins
    • D.J. Craik Plant cyclotides: circular, knotted peptide toxins Toxicon 39 2001 1809 1813
    • (2001) Toxicon , vol.39 , pp. 1809-1813
    • Craik, D.J.1
  • 12
    • 0035845584 scopus 로고    scopus 로고
    • Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis
    • C. Jennings, J. West, C. Waine, D.J. Craik, and M. Anderson Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis Proc. Natl Acad. Sci. USA 98 2001 10614 10619
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10614-10619
    • Jennings, C.1    West, J.2    Waine, C.3    Craik, D.J.4    Anderson, M.5
  • 13
    • 0000014794 scopus 로고
    • An oxytocic principle found in Oldenlandia affinis DC
    • L. Gran An oxytocic principle found in Oldenlandia affinis DC Meddelelser Norsk Farmaceutisk Selskap 32 1970 138 173
    • (1970) Meddelelser Norsk Farmaceutisk Selskap , vol.32 , pp. 138-173
    • Gran, L.1
  • 14
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uteronic polypeptide kalata B1
    • O. Saether, D.J. Craik, I.D. Campbell, K. Sletten, J. Juul, and D.G. Norman Elucidation of the primary and three-dimensional structure of the uteronic polypeptide kalata B1 Biochemistry 34 1995 4147 4158
    • (1995) Biochemistry , vol.34 , pp. 4147-4158
    • Saether, O.1    Craik, D.J.2    Campbell, I.D.3    Sletten, K.4    Juul, J.5    Norman, D.G.6
  • 15
    • 0015817287 scopus 로고
    • Oxytocic principles of Oldenlandia affinis
    • L. Gran Oxytocic principles of Oldenlandia affinis Lloydia 36 1973 174 178
    • (1973) Lloydia , vol.36 , pp. 174-178
    • Gran, L.1
  • 16
    • 0028036769 scopus 로고
    • Circulins a and B. Novel human immunodeficiency virus (HIV)-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia
    • K.R. Gustafson, R.C. Sowder, L.E. Henderson, I.C. Parsons, Y. Kashman, and J.H. Cardellina Circulins A and B. Novel human immunodeficiency virus (HIV)-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia J. Am. Chem. Soc. 116 1994 9337 9338
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9337-9338
    • Gustafson, K.R.1    Sowder, R.C.2    Henderson, L.E.3    Parsons, I.C.4    Kashman, Y.5    Cardellina, J.H.6
  • 17
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
    • J.P. Tam, Y.A. Lu, J.L. Yang, and K.W. Chiu An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides Proc. Natl Acad. Sci. USA 96 1999 8913 8918
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8913-8918
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3    Chiu, K.W.4
  • 20
    • 0027177567 scopus 로고
    • Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray
    • T. Schöpke, M.I. Hasan Agha, R. Kraft, A. Otto, and K. Hiller Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray Sci. Pharmaceut. 61 1993 145 153
    • (1993) Sci. Pharmaceut. , vol.61 , pp. 145-153
    • Schöpke, T.1    Hasan Agha, M.I.2    Kraft, R.3    Otto, A.4    Hiller, K.5
  • 21
    • 33645033202 scopus 로고    scopus 로고
    • A continent of plant defense peptide diversity: Cyclotides in Australian Hybanthus (Violaceae)
    • S. Simonsen, L. Sando, D.C. Ireland, M.L. Colgrave, and D.J. Craik A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae) Plant Cell 17 2005 3176 3189
    • (2005) Plant Cell , vol.17 , pp. 3176-3189
    • Simonsen, S.1    Sando, L.2    Ireland, D.C.3    Colgrave, M.L.4    Craik, D.J.5
  • 23
    • 0038492655 scopus 로고    scopus 로고
    • Structures of naturally occuring circular proteins from bacteria
    • D.J. Craik, N.L. Daly, I. Saska, M. Trabi, and K.J. Rosengren Structures of naturally occuring circular proteins from bacteria J. Bacteriol. 185 2003 4011 4021
    • (2003) J. Bacteriol. , vol.185 , pp. 4011-4021
    • Craik, D.J.1    Daly, N.L.2    Saska, I.3    Trabi, M.4    Rosengren, K.J.5
  • 24
    • 8744227077 scopus 로고    scopus 로고
    • Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins
    • J.L. Dutton, R.F. Renda, C. Waine, R.J. Clark, N.L. Daly, and C. Jennings Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins J. Biol. Chem. 279 2004 46858 46867
    • (2004) J. Biol. Chem. , vol.279 , pp. 46858-46867
    • Dutton, J.L.1    Renda, R.F.2    Waine, C.3    Clark, R.J.4    Daly, N.L.5    Jennings, C.6
  • 25
    • 0031609083 scopus 로고    scopus 로고
    • Function of bacterial propeptides
    • P. Braun, and J. Tommassen Function of bacterial propeptides Trends Microbiol. 6 1998 6 8
    • (1998) Trends Microbiol. , vol.6 , pp. 6-8
    • Braun, P.1    Tommassen, J.2
  • 26
    • 20444441123 scopus 로고    scopus 로고
    • Isolation and characterization of novel cyclotides from Viola hederaceae: Solution structure and anti-HIV activity of vhl-1, a leaf specific expressed cyclotide
    • B. Chen, M.L. Colgrave, N.L. Daly, K.J. Rosengren, K.R. Gustafson, and D.J. Craik Isolation and characterization of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf specific expressed cyclotide J. Biol. Chem. 280 2005 22395 22405
    • (2005) J. Biol. Chem. , vol.280 , pp. 22395-22405
    • Chen, B.1    Colgrave, M.L.2    Daly, N.L.3    Rosengren, K.J.4    Gustafson, K.R.5    Craik, D.J.6
  • 28
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • D.S. Wishart, B.D. Sykes, and F.M. Richards The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy Biochemistry 31 1992 1647 1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 29
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG J. Biomol. NMR 5 1995 14 24
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 30
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyse structural motifs in proteins
    • E.G. Hutchinson, and J.M. Thornton PROMOTIF: a program to identify and analyse structural motifs in proteins Protein Sci. 5 1996 212 220
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 31
    • 2442715239 scopus 로고    scopus 로고
    • Thermal, chemical and enzymatic stability of the cyclotide kalata B1: The importance of the cyclic cystine knot
    • M.L. Colgrave, and D.J. Craik Thermal, chemical and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot Biochemistry 43 2004 5965 5975
    • (2004) Biochemistry , vol.43 , pp. 5965-5975
    • Colgrave, M.L.1    Craik, D.J.2
  • 32
    • 0034705410 scopus 로고    scopus 로고
    • Acyclic permutants of naturally occuring cyclic proteins
    • N.L. Daly, and D.J. Craik Acyclic permutants of naturally occuring cyclic proteins J. Biol. Chem. 275 2000 19068 19075
    • (2000) J. Biol. Chem. , vol.275 , pp. 19068-19075
    • Daly, N.L.1    Craik, D.J.2
  • 35
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • L. Braunschweiler, and R.R. Ernst Coherence transfer by isotropic mixing: application to proton correlation spectroscopy J. Magn. Reson. 53 1983 521 528
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 36
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • A. Bax, and D.G. Davis MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy J. Magn. Reson. 65 1985 355 360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 37
    • 0345311136 scopus 로고
    • Practical aspects of the E.COSY technique, measurement of scalar spin-spin coupling constants in peptides
    • C. Griesinger, O.W. Sørensen, and R.R. Ernst Practical aspects of the E.COSY technique, measurement of scalar spin-spin coupling constants in peptides J. Magn. Reson. 75 1987 474 492
    • (1987) J. Magn. Reson. , vol.75 , pp. 474-492
    • Griesinger, C.1    Sørensen, O.W.2    Ernst, R.R.3
  • 38
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • J. Jenner, B.H. Meier, P. Bachmann, and R.R. Ernst Investigation of exchange processes by two-dimensional NMR spectroscopy J. Chem. Phys. 71 1979 4546 4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jenner, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 39
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J. Biomol. NMR 2 1992 661 665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 40
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • P. Güntert, C. Mumenthaler, and K. Wüthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 41
    • 0031569392 scopus 로고    scopus 로고
    • New applications of simulated annealing in X-ray crystallography and solution NMR
    • A.T. Brünger, P.D. Adams, and L.M. Rice New applications of simulated annealing in X-ray crystallography and solution NMR Structure 5 1997 325 336
    • (1997) Structure , vol.5 , pp. 325-336
    • Brünger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 42
    • 0033064496 scopus 로고    scopus 로고
    • Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
    • J.P. Linge, and M. Nilges Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation J. Biomol. NMR 13 1999 51 59
    • (1999) J. Biomol. NMR , vol.13 , pp. 51-59
    • Linge, J.P.1    Nilges, M.2
  • 43
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmann, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.