메뉴 건너뛰기




Volumn 79, Issue 5, 2011, Pages 1538-1549

NMR solution structure of a cyanovirin homolog from wheat head blight fungus

Author keywords

Antiviral protein; CVNH; HIV; Lectin; NMR solution structure

Indexed keywords

CYANOVIRIN N;

EID: 79954623874     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22981     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 0015510673 scopus 로고
    • Lectins: cell-agglutinating and sugar-specific proteins
    • Sharon N, Lis H. Lectins: cell-agglutinating and sugar-specific proteins. Science 1972; 177: 949-959.
    • (1972) Science , vol.177 , pp. 949-959
    • Sharon, N.1    Lis, H.2
  • 2
    • 0023191455 scopus 로고
    • Bacterial lectins, cell-cell recognition and infectious disease
    • Sharon N. Bacterial lectins, cell-cell recognition and infectious disease. FEBS Lett 1987; 217: 145-157.
    • (1987) FEBS Lett , vol.217 , pp. 145-157
    • Sharon, N.1
  • 3
    • 7244234285 scopus 로고    scopus 로고
    • Immunolocalization and functional role of Sclerotium rolfsii lectin in development of fungus by interaction with its endogenous receptor
    • Swamy BM, Bhat AG, Hegde GV, Naik RS, Kulkarni S, Inamdar SR. Immunolocalization and functional role of Sclerotium rolfsii lectin in development of fungus by interaction with its endogenous receptor. Glycobiology 2004; 14: 951-957.
    • (2004) Glycobiology , vol.14 , pp. 951-957
    • Swamy, B.M.1    Bhat, A.G.2    Hegde, G.V.3    Naik, R.S.4    Kulkarni, S.5    Inamdar, S.R.6
  • 4
    • 24644437812 scopus 로고    scopus 로고
    • The anti-HIV cyanovirin-N domain is evolutionarily conserved and occurs as a protein module in eukaryotes
    • Percudani R, Montanini B, Ottonello S. The anti-HIV cyanovirin-N domain is evolutionarily conserved and occurs as a protein module in eukaryotes. Proteins 2005; 60: 670-678.
    • (2005) Proteins , vol.60 , pp. 670-678
    • Percudani, R.1    Montanini, B.2    Ottonello, S.3
  • 6
    • 41449109826 scopus 로고    scopus 로고
    • The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity
    • Koharudin LM, Viscomi AR, Jee JG, Ottonello S, Gronenborn AM. The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity. Structure 2008; 16: 570-584.
    • (2008) Structure , vol.16 , pp. 570-584
    • Koharudin, L.M.1    Viscomi, A.R.2    Jee, J.G.3    Ottonello, S.4    Gronenborn, A.M.5
  • 9
    • 33845632976 scopus 로고    scopus 로고
    • Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition
    • Barrientos LG, Matei E, Lasala F, Delgado R, Gronenborn AM. Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition. Protein Eng Des Sel 2006; 19: 525-535.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 525-535
    • Barrientos, L.G.1    Matei, E.2    Lasala, F.3    Delgado, R.4    Gronenborn, A.M.5
  • 10
    • 34547916495 scopus 로고    scopus 로고
    • A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity
    • Fromme R, Katiliene Z, Giomarelli B, Bogani F, Mc Mahon J, Mori T, Fromme P, Ghirlanda G. A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity. Biochemistry 2007; 46: 9199-9207.
    • (2007) Biochemistry , vol.46 , pp. 9199-9207
    • Fromme, R.1    Katiliene, Z.2    Giomarelli, B.3    Bogani, F.4    Mc Mahon, J.5    Mori, T.6    Fromme, P.7    Ghirlanda, G.8
  • 11
    • 48149091784 scopus 로고    scopus 로고
    • Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping
    • Matei E, Furey W, Gronenborn AM. Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping. Structure 2008; 16: 1183-1194.
    • (2008) Structure , vol.16 , pp. 1183-1194
    • Matei, E.1    Furey, W.2    Gronenborn, A.M.3
  • 12
    • 77951219869 scopus 로고    scopus 로고
    • Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization
    • Matei E, Zheng A, Furey W, Rose J, Aiken C, Gronenborn AM. Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization. J Biol Chem; 285: 13057-13065.
    • J Biol Chem , vol.285 , pp. 13057-13065
    • Matei, E.1    Zheng, A.2    Furey, W.3    Rose, J.4    Aiken, C.5    Gronenborn, A.M.6
  • 13
    • 3843048994 scopus 로고    scopus 로고
    • Breeding for resistance to Fusarium head blight of wheat in China
    • In: Leonard KJ,Bushnell WR, editors. Fusarium head blight of wheat and barley. St Paul, MN: APS Press.
    • Bai GH, Chen LF, Shaner GE. Breeding for resistance to Fusarium head blight of wheat in China. In: Leonard KJ, Bushnell WR, editors. Fusarium head blight of wheat and barley. St Paul, MN: APS Press; 2003. pp 296-317.
    • (2003) , pp. 296-317
    • Bai, G.H.1    Chen, L.F.2    Shaner, G.E.3
  • 17
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson BA. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 2004; 278: 313-352.
    • (2004) Methods Mol Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 18
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A, Grzesiek S. Methodological advances in protein NMR. Acc Chem Res 1993; 26: 131-138.
    • (1993) Acc Chem Res , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 19
    • 0025361336 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromolecules
    • Fesik SW, Zuiderweg ER. Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromolecules. Q Rev Biophys 1990; 23: 97-131.
    • (1990) Q Rev Biophys , vol.23 , pp. 97-131
    • Fesik, S.W.1    Zuiderweg, E.R.2
  • 20
    • 0027636003 scopus 로고
    • A simple and sensitive experiment for measurement of JCC couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins
    • Grzesiek S, Vuister GW, Bax A. A simple and sensitive experiment for measurement of JCC couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins. J Biomol NMR 1993; 3: 487-493.
    • (1993) J Biomol NMR , vol.3 , pp. 487-493
    • Grzesiek, S.1    Vuister, G.W.2    Bax, A.3
  • 21
    • 0027568083 scopus 로고
    • A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments
    • Logan TM, Olejniczak ET, Xu RX, Fesik SW. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments. J Biomol NMR 1993; 3: 225-231.
    • (1993) J Biomol NMR , vol.3 , pp. 225-231
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 22
    • 0002522872 scopus 로고
    • A Simultaneous 15N, 1H-HSQC and 13C, 1H-HSQC with sensitivity enhancement and a heteronuclear gradient-echo
    • Sattler M, Maurer M, Schleucher J, Griesinger C. A Simultaneous 15N, 1H-HSQC and 13C, 1H-HSQC with sensitivity enhancement and a heteronuclear gradient-echo. J Biomol NMR 1995; 5: 97-102.
    • (1995) J Biomol NMR , vol.5 , pp. 97-102
    • Sattler, M.1    Maurer, M.2    Schleucher, J.3    Griesinger, C.4
  • 23
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Guntert P, Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 2002; 319: 209-227.
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 24
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 1997; 273: 283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 25
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 1999; 13: 289-302.
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 27
  • 29
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997; 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 31
    • 34247135950 scopus 로고    scopus 로고
    • A mutation in alpha helix 3 of CA renders human immunodeficiency virus type 1 cyclosporin A resistant and dependent: rescue by a second-site substitution in a distal region of CA
    • Yang RAiken C. A mutation in alpha helix 3 of CA renders human immunodeficiency virus type 1 cyclosporin A resistant and dependent: rescue by a second-site substitution in a distal region of CA. J Virol 2007; 81: 3749-3756.
    • (2007) J Virol , vol.81 , pp. 3749-3756
    • Yang, R.1    Aiken, C.2
  • 32
    • 0034799906 scopus 로고    scopus 로고
    • The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV envelope protein gp120
    • Bewley CA, Otero-Quintero S. The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV envelope protein gp120. J Am Chem Soc 2001; 123: 3892-3902.
    • (2001) J Am Chem Soc , vol.123 , pp. 3892-3902
    • Bewley, C.A.1    Otero-Quintero, S.2
  • 33
    • 0036773694 scopus 로고    scopus 로고
    • Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: calorimetric and NMR characterization
    • Shenoy SR, Barrientos LG, Ratner DM, O'Keefe BR, Seeberger PH, Gronenborn AM, Boyd MR. Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: calorimetric and NMR characterization. Chem Biol 2002; 9: 1109-1118.
    • (2002) Chem Biol , vol.9 , pp. 1109-1118
    • Shenoy, S.R.1    Barrientos, L.G.2    Ratner, D.M.3    O'Keefe, B.R.4    Seeberger, P.H.5    Gronenborn, A.M.6    Boyd, M.R.7
  • 35
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thoronton JM. Disulphide bridges in globular proteins. J Mol Biol 1981; 151: 261-287.
    • (1981) J Mol Biol , vol.151 , pp. 261-287
    • Thoronton, J.M.1
  • 36
    • 0031559765 scopus 로고    scopus 로고
    • Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyanobacterium Nostoc ellipsosporum
    • Gustafson KR, Sowder RC, II, Henderson LE, Cardellina JH, II, McMahon JB, Rajamani U, Pannell LK, Boyd MR. Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyanobacterium Nostoc ellipsosporum. Biochem Biophys Res Commun 1997; 238: 223-228.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 223-228
    • Gustafson, K.R.1    Sowder II, R.C.2    Henderson, L.E.3    Cardellina II, J.H.4    McMahon, J.B.5    Rajamani, U.6    Pannell, L.K.7    Boyd, M.R.8
  • 40
    • 43049111403 scopus 로고    scopus 로고
    • Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution
    • Fromme R, Katiliene Z, Fromme P, Ghirlanda G. Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution. Protein Sci 2008; 17: 939-944.
    • (2008) Protein Sci , vol.17 , pp. 939-944
    • Fromme, R.1    Katiliene, Z.2    Fromme, P.3    Ghirlanda, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.