메뉴 건너뛰기




Volumn 585, Issue 2, 2011, Pages 300-306

Ultra-high resolution crystal structure of a dimeric defensin SPE10

Author keywords

Crystal structure; Defensin; Dimer; Mechanism; Ultra high resolution

Indexed keywords

ARGININE; DEFENSIN; PROTEIN SPE10; UNCLASSIFIED DRUG;

EID: 78651349903     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.12.039     Document Type: Article
Times cited : (28)

References (50)
  • 1
    • 27144504220 scopus 로고    scopus 로고
    • Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus
    • P.H. Mygind Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus Nature 437 2005 975 980
    • (2005) Nature , vol.437 , pp. 975-980
    • Mygind, P.H.1
  • 2
    • 0033569408 scopus 로고    scopus 로고
    • Beta-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6
    • D. Yang Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6 Science 286 1999 525 528
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1
  • 3
    • 78651372548 scopus 로고    scopus 로고
    • The current status of the practice of radiofrequency in the world
    • P.P. Raj, and S. Erdine The current status of the practice of radiofrequency in the world Pain Pract. 2 2002 176 179
    • (2002) Pain Pract. , vol.2 , pp. 176-179
    • Raj, P.P.1    Erdine, S.2
  • 4
    • 67349088413 scopus 로고    scopus 로고
    • Plant defensins - Prospects for the biological functions and biotechnological properties
    • O. Carvalho Ade, and V.M. Gomes Plant defensins - prospects for the biological functions and biotechnological properties Peptides 30 2009 1007 1020
    • (2009) Peptides , vol.30 , pp. 1007-1020
    • Carvalho Ade, O.1    Gomes, V.M.2
  • 5
    • 77952632254 scopus 로고    scopus 로고
    • Structural aspects of plant antimicrobial peptides
    • L. Padovan, M. Scocchi, and A. Tossi Structural aspects of plant antimicrobial peptides Curr. Protein Pept. Sci. 11 2010 210 219
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 210-219
    • Padovan, L.1    Scocchi, M.2    Tossi, A.3
  • 6
    • 0028271965 scopus 로고
    • Pseudothionin-St1, a potato peptide active against potato pathogens
    • DOI 10.1111/j.1432-1033.1994.tb18974.x
    • M. Moreno, A. Segura, and F. Garcia-Olmedo Pseudothionin-St1, a potato peptide active against potato pathogens Eur. J. Biochem. 223 1994 135 139 (Pubitemid 24221654)
    • (1994) European Journal of Biochemistry , vol.223 , Issue.1 , pp. 135-139
    • Moreno, M.1    Segura, A.2    Garcia-Olmedo, F.3
  • 7
    • 0029014273 scopus 로고
    • Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae
    • R.W. Osborn Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae FEBS Lett. 368 1995 257 262
    • (1995) FEBS Lett. , vol.368 , pp. 257-262
    • Osborn, R.W.1
  • 8
    • 0032544607 scopus 로고    scopus 로고
    • Novel defensin subfamily from spinach (Spinacia oleracea)
    • DOI 10.1016/S0014-5793(98)01060-6, PII S0014579398010606
    • A. Segura, M. Moreno, A. Molina, and F. Garcia-Olmedo Novel defensin subfamily from spinach (Spinacia oleracea) FEBS Lett. 435 1998 159 162 (Pubitemid 28434991)
    • (1998) FEBS Letters , vol.435 , Issue.2-3 , pp. 159-162
    • Segura, A.1    Moreno, M.2    Molina, A.3    Garcia-Olmedo, F.4
  • 9
    • 0032005344 scopus 로고    scopus 로고
    • Antimicrobial peptides of vertebrates
    • DOI 10.1016/S0952-7915(98)80029-0
    • T. Ganz, and R.I. Lehrer Antimicrobial peptides of vertebrates Curr. Opin. Immunol. 10 1998 41 44 (Pubitemid 28112077)
    • (1998) Current Opinion in Immunology , vol.10 , Issue.1 , pp. 41-44
    • Ganz, T.1    Lehrer, R.I.2
  • 10
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • DOI 10.1016/S0952-7915(99)80005-3
    • R.I. Lehrer, and T. Ganz Antimicrobial peptides in mammalian and insect host defence Curr. Opin. Immunol. 11 1999 23 27 (Pubitemid 29082332)
    • (1999) Current Opinion in Immunology , vol.11 , Issue.1 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 11
    • 0033668495 scopus 로고    scopus 로고
    • Fungal pathogen protection in potato by expression of a plant defensin peptide
    • A.G. Gao Fungal pathogen protection in potato by expression of a plant defensin peptide Nat. Biotechnol. 18 2000 1307 1310
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1307-1310
    • Gao, A.G.1
  • 12
    • 0033763238 scopus 로고    scopus 로고
    • Transgenic plants expressing cationic peptide chimeras exhibit broad-spectrum resistance to phytopathogens
    • M. Osusky, G. Zhou, L. Osuska, R.E. Hancock, W.W. Kay, and S. Misra Transgenic plants expressing cationic peptide chimeras exhibit broad-spectrum resistance to phytopathogens Nat. Biotechnol. 18 2000 1162 1166
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1162-1166
    • Osusky, M.1    Zhou, G.2    Osuska, L.3    Hancock, R.E.4    Kay, W.W.5    Misra, S.6
  • 13
    • 0029294060 scopus 로고
    • Small cysteine-rich antifungal proteins from radish: Their role in host defense
    • F.R. Terras Small cysteine-rich antifungal proteins from radish: their role in host defense Plant Cell 7 1995 573 588
    • (1995) Plant Cell , vol.7 , pp. 573-588
    • Terras, F.R.1
  • 14
    • 28544434796 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex
    • DOI 10.1021/bi051656d
    • L. Yu, C. Sun, D. Song, J. Shen, N. Xu, A. Gunasekera, P.J. Hajduk, and E.T. Olejniczak Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex Biochemistry 44 2005 15834 15841 (Pubitemid 41746914)
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15834-15841
    • Yu, L.1    Sun, C.2    Song, D.3    Shen, J.4    Xu, N.5    Gunasekera, A.6    Hajduk, P.J.7    Olejniczak, E.T.8
  • 17
    • 0030750976 scopus 로고    scopus 로고
    • Solution structure of drosomycin, the first inducible antifungal protein from insects
    • C. Landon, P. Sodano, C. Hetru, J. Hoffmann, and M. Ptak Solution structure of drosomycin, the first inducible antifungal protein from insects Protein Sci. 6 1997 1878 1884 (Pubitemid 27391268)
    • (1997) Protein Science , vol.6 , Issue.9 , pp. 1878-1884
    • Landon, C.1    Sodano, P.2    Hetru, C.3    Hoffmann, J.4    Ptak, M.5
  • 18
    • 4444295137 scopus 로고    scopus 로고
    • Differential antifungal and calcium channel-blocking activity among structurally related plant defensins
    • DOI 10.1104/pp.104.040873
    • R.G. Spelbrink, N. Dilmac, A. Allen, T.J. Smith, D.M. Shah, and G.H. Hockerman Differential antifungal and calcium channel-blocking activity among structurally related plant defensins Plant Physiol. 135 2004 2055 2067 (Pubitemid 39182785)
    • (2004) Plant Physiology , vol.135 , Issue.4 , pp. 2055-2067
    • Spelbrink, R.G.1    Dilmac, N.2    Allen, A.3    Smith, T.J.4    Shah, D.M.5    Hockerman, G.H.6
  • 20
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • DOI 10.1038/nri1180
    • T. Ganz Defensins: antimicrobial peptides of innate immunity Nat. Rev. Immunol. 3 2003 710 720 (Pubitemid 41070812)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 21
    • 0030871334 scopus 로고    scopus 로고
    • Differential effects of five types of antipathogenic plant peptides on model membranes
    • DOI 10.1016/S0014-5793(97)00613-3, PII S0014579397006133
    • J.M. Caaveiro, A. Molina, J.M. Gonzalez-Manas, P. Rodriguez-Palenzuela, F. Garcia-Olmedo, and F.M. Goni Differential effects of five types of antipathogenic plant peptides on model membranes FEBS Lett. 410 1997 338 342 (Pubitemid 27304092)
    • (1997) FEBS Letters , vol.410 , Issue.2-3 , pp. 338-342
    • Caaveiro, J.M.M.1    Molina, A.2    Gonzalez-Manas, J.M.3    Rodriguez-Palenzuela, P.4    Garcia-Olmedo, F.5    Goni, F.M.6
  • 25
    • 0032751756 scopus 로고    scopus 로고
    • Permeabilization of fungal membranes by plant defensins inhibits fungal growth
    • K. Thevissen, F.R. Terras, and W.F. Broekaert Permeabilization of fungal membranes by plant defensins inhibits fungal growth Appl. Environ. Microbiol. 65 1999 5451 5458 (Pubitemid 129520636)
    • (1999) Applied and Environmental Microbiology , vol.65 , Issue.12 , pp. 5451-5458
    • Thevissen, K.1    Terras, F.R.G.2    Broekaert, W.F.3
  • 26
    • 0031465590 scopus 로고    scopus 로고
    • Specific, high affinity binding sites for an antifungal plant defensin on Neurospora crassa hyphae and microsomal membranes
    • DOI 10.1074/jbc.272.51.32176
    • K. Thevissen, R.W. Osborn, D.P. Acland, and W.F. Broekaert Specific, high affinity binding sites for an antifungal plant defensin on Neurospora crassa hyphae and microsomal membranes J. Biol. Chem. 272 1997 32176 32181 (Pubitemid 28011892)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 32176-32181
    • Thevissen, K.1    Osborn, R.W.2    Acland, D.P.3    Broekaert, W.F.4
  • 27
    • 15644372264 scopus 로고    scopus 로고
    • Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity
    • G.W. De Samblanx Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity J. Biol. Chem. 272 1997 1171 1179
    • (1997) J. Biol. Chem. , vol.272 , pp. 1171-1179
    • De Samblanx, G.W.1
  • 28
    • 0029113242 scopus 로고
    • Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry
    • A.M. Krezel, C. Kasibhatla, P. Hidalgo, R. MacKinnon, and G. Wagner Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry Protein Sci. 4 1995 1478 1489
    • (1995) Protein Sci. , vol.4 , pp. 1478-1489
    • Krezel, A.M.1    Kasibhatla, C.2    Hidalgo, P.3    MacKinnon, R.4    Wagner, G.5
  • 30
    • 19344362065 scopus 로고    scopus 로고
    • The multitude of targets for the immune system and drug therapy in the fungal cell wall
    • DOI 10.1016/j.micinf.2005.03.002, PII S1286457905000572
    • L. Nimrichter, M.L. Rodrigues, E.G. Rodrigues, and L.R. Travassos The multitude of targets for the immune system and drug therapy in the fungal cell wall Microb. Infect. 7 2005 789 798 (Pubitemid 40720434)
    • (2005) Microbes and Infection , vol.7 , Issue.4 , pp. 789-798
    • Nimrichter, L.1    Rodrigues, M.L.2    Rodrigues, E.G.3    Travassos, L.R.4
  • 33
    • 17844363007 scopus 로고    scopus 로고
    • CDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds
    • DOI 10.1007/s11103-004-6637-y
    • X. Song, J. Wang, F. Wu, X. Li, M. Teng, and W. Gong CDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds Plant Mol. Biol. 57 2005 13 20 (Pubitemid 40580439)
    • (2005) Plant Molecular Biology , vol.57 , Issue.1 , pp. 13-20
    • Song, X.1    Wang, J.2    Wu, F.3    Li, X.4    Teng, M.5    Gong, W.6
  • 34
    • 16644369026 scopus 로고    scopus 로고
    • Purification, characterization and preliminary crystallographic studies of a novel plant defensin from Pachyrrhizus erosus seeds
    • DOI 10.1107/S0907444904007395
    • X. Song, Z. Zhou, J. Wang, F. Wu, and W. Gong Purification, characterization and preliminary crystallographic studies of a novel plant defensin from Pachyrrhizus erosus seeds Acta Crystallogr. D: Biol. Crystallogr. 60 2004 1121 1124 (Pubitemid 41295455)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.6 , pp. 1121-1124
    • Song, X.1    Zhou, Z.2    Wang, J.3    Wu, F.4    Gong, W.5
  • 36
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • DOI 10.1107/S0907444902018036
    • T.C. Terwilliger Automated main-chain model building by template matching and iterative fragment extension Acta Crystallogr. D: Biol. Crystallogr. 59 2003 38 44 (Pubitemid 36117204)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.1 , pp. 38-44
    • Terwilliger, T.C.1
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 Pt. 2 1991 110 119
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • V.B. Chen MolProbity: all-atom structure validation for macromolecular crystallography Acta Crystallogr. D: Biol. Crystallogr. 66 2010 12 21
    • (2010) Acta Crystallogr. D: Biol. Crystallogr. , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 41
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • DOI 10.1038/364412a0
    • K.L. Clark, E.D. Halay, E. Lai, and S.K. Burley Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5 Nature 364 1993 412 420 (Pubitemid 23263212)
    • (1993) Nature , vol.364 , Issue.6436 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 42
    • 0027423758 scopus 로고
    • Crystal structure of a five-finger GLI-DNA complex: New perspectives on zinc fingers
    • N.P. Pavletich, and C.O. Pabo Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers Science 261 1993 1701 1707
    • (1993) Science , vol.261 , pp. 1701-1707
    • Pavletich, N.P.1    Pabo, C.O.2
  • 43
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1
    • N.P. Pavletich, and C.O. Pabo Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Science 252 1991 809 817
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2
  • 44
    • 48249157851 scopus 로고    scopus 로고
    • Biomolecular engineering by combinatorial design and high-throughput screening: Small, soluble peptides that permeabilize membranes
    • R. Rathinakumar, and W.C. Wimley Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes J. Am. Chem. Soc. 130 2008 9849 9858
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9849-9858
    • Rathinakumar, R.1    Wimley, W.C.2
  • 49
    • 0036301039 scopus 로고    scopus 로고
    • Solution structure of Pisum sativum defensin 1 by high resolution NMR: Plant defensins, identical backbone with different mechanisms of action
    • DOI 10.1006/jmbi.2001.5252
    • M.S. Almeida, K.M. Cabral, E. Kurtenbach, F.C. Almeida, and A.P. Valente Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action J. Mol. Biol. 315 2002 749 757 (Pubitemid 34729323)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.4 , pp. 749-757
    • Almeida, M.S.1    Cabral, K.M.S.2    Kurtenbach, E.3    Almeida, F.C.L.4    Valente, A.P.5
  • 50
    • 78549295936 scopus 로고    scopus 로고
    • Permeabilization of fungal hyphae by the plant defensin NaD1 occurs through a cell wall dependent process
    • N.L. van der Weerden, R.E. Hancock, and M.A. Anderson Permeabilization of fungal hyphae by the plant defensin NaD1 occurs through a cell wall dependent process J. Biol. Chem. 285 2010 37513 37520
    • (2010) J. Biol. Chem. , vol.285 , pp. 37513-37520
    • Van Der Weerden, N.L.1    Hancock, R.E.2    Anderson, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.