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Volumn 18, Issue 7, 2009, Pages 1498-1506

Alanine substitutions of noncysteine residues in the cysteine-stabilized αβ motif

Author keywords

amylase; Alanine scan; Circular dichroism spectroscopy; Fluorescence spectroscopy; Plant defensin; Protein engineering

Indexed keywords

ALANINE; CYSTEINE; DEFENSIN; MUTANT PROTEIN; UNCLASSIFIED DRUG; VIGNA RADIATE DEFENSIN 1;

EID: 67650076198     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.164     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 24944450680 scopus 로고    scopus 로고
    • Artificial, non-antibody binding proteins for pharmaceutical and industrial applications
    • Hey T, Fiedler E, Rudolph R, Fiedler M (2005) Artificial, non-antibody binding proteins for pharmaceutical and industrial applications. Trends Biotechnol 23:514-522.
    • (2005) Trends Biotechnol , vol.23 , pp. 514-522
    • Hey, T.1    Fiedler, E.2    Rudolph, R.3    Fiedler, M.4
  • 3
    • 34548522063 scopus 로고    scopus 로고
    • Alternative non-antibody scaffolds for molecular recognition
    • Skerra A (2007) Alternative non-antibody scaffolds for molecular recognition. Curr Opin Biotechnol 18:295-304.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 295-304
    • Skerra, A.1
  • 4
    • 33746536641 scopus 로고    scopus 로고
    • Engineering of β-propeller protein scaffolds by multiple gene duplication and fusion of an idealized WD repeat
    • Nikkhah M, Jawad-Alami Z, Demydchuk M, Ribbons D, Paoli M (2006) Engineering of β-propeller protein scaffolds by multiple gene duplication and fusion of an idealized WD repeat. Biomol Eng 23:185-194.
    • (2006) Biomol Eng , vol.23 , pp. 185-194
    • Nikkhah, M.1    Jawad-Alami, Z.2    Demydchuk, M.3    Ribbons, D.4    Paoli, M.5
  • 5
    • 18044364063 scopus 로고    scopus 로고
    • Rapid creation of a novel protein function by in vitro coevolution
    • Chen Z, Zhao H (2005) Rapid creation of a novel protein function by in vitro coevolution. J Mol Biol 348: 1273-1282.
    • (2005) J Mol Biol , vol.348 , pp. 1273-1282
    • Chen, Z.1    Zhao, H.2
  • 6
    • 0034656399 scopus 로고    scopus 로고
    • Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein
    • Assadi-Porter FM, Aceti DJ, Markley JL (2000) Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein. Arch Biochem Biophys 376: 259-265.
    • (2000) Arch Biochem Biophys , vol.376 , pp. 259-265
    • Assadi-Porter, F.M.1    Aceti, D.J.2    Markley, J.L.3
  • 8
    • 0036829766 scopus 로고    scopus 로고
    • Roles of disulfide bridges in scorpion toxin BmK M1 analyzed by mutagenesis
    • Sun YM, Liu W, Zhu RH, Wang DC, Goudet C, Tytgat J (2002) Roles of disulfide bridges in scorpion toxin BmK M1 analyzed by mutagenesis. J Pept Res 60:247-256.
    • (2002) J Pept Res , vol.60 , pp. 247-256
    • Sun, Y.M.1    Liu, W.2    Zhu, R.H.3    Wang, D.C.4    Goudet, C.5    Tytgat, J.6
  • 9
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 10
    • 27144432006 scopus 로고    scopus 로고
    • Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily
    • Zhu S, Gao B, Tytgat J (2005) Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily. Cell Mol Life Sci 62:2257-2269.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2257-2269
    • Zhu, S.1    Gao, B.2    Tytgat, J.3
  • 12
    • 1942485914 scopus 로고    scopus 로고
    • Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin inhibitor genes
    • Clauss MJ, Mitchell-Olds T (2004) Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin inhibitor genes. Genetics 166:1419-1436.
    • (2004) Genetics , vol.166 , pp. 1419-1436
    • Clauss, M.J.1    Mitchell-Olds, T.2
  • 13
    • 20444406094 scopus 로고    scopus 로고
    • Sesquin, a potent defensin-like antimicrobial peptide from ground beans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase
    • Wong JH, Ng TB (2005) Sesquin, a potent defensin-like antimicrobial peptide from ground beans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase. Peptides 26:1120-1126.
    • (2005) Peptides , vol.26 , pp. 1120-1126
    • Wong, J.H.1    Ng, T.B.2
  • 14
    • 4444295137 scopus 로고    scopus 로고
    • Differential antifungal and calcium channel-blocking activity among structurally related plant defensins
    • Spelbrink RG, Dilmac N, Allen A, Smith TJ, Shah DM, Hockerman GH (2004) Differential antifungal and calcium channel-blocking activity among structurally related plant defensins. Plant Physiol 135:2055-2067.
    • (2004) Plant Physiol , vol.135 , 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
  • 15
    • 17844363007 scopus 로고    scopus 로고
    • cDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds
    • Song X, Wang J, Wu F, Li X, Teng M, Gong W (2005) cDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds. Plant Mol Biol 57:13-20.
    • (2005) Plant Mol Biol , vol.57 , pp. 13-20
    • Song, X.1    Wang, J.2    Wu, F.3    Li, X.4    Teng, M.5    Gong, W.6
  • 17
    • 33745304784 scopus 로고    scopus 로고
    • Plant thionins-the structural perspective
    • Stec B (2006) Plant thionins-the structural perspective. Cell Mol Life Sci 63:1370-1385.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1370-1385
    • Stec, B.1
  • 18
    • 34250887046 scopus 로고    scopus 로고
    • Structure-based protein engineering for α-amylase inhibitory activity of plant defensin
    • Lin KF, Lee TR, Tsai PH, Hsu MP, Chen CS, Lyu PC (2007) Structure-based protein engineering for α-amylase inhibitory activity of plant defensin. Proteins 68:530-540.
    • (2007) Proteins , vol.68 , pp. 530-540
    • Lin, K.F.1    Lee, T.R.2    Tsai, P.H.3    Hsu, M.P.4    Chen, C.S.5    Lyu, P.C.6
  • 19
    • 0029050766 scopus 로고
    • Scorpion toxins as natural scaffolds for protein engineering
    • Vita C, Roumestand C, Toma F, Menez A (1995) Scorpion toxins as natural scaffolds for protein engineering. Proc Natl Acad Sci USA 92:6404-6408.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6404-6408
    • Vita, C.1    Roumestand, C.2    Toma, F.3    Menez, A.4
  • 23
    • 67650073705 scopus 로고    scopus 로고
    • The proteins of plant defensin family and their application beyond plant disease control
    • Yang Y-F, Lyu P-C (2008) The proteins of plant defensin family and their application beyond plant disease control. Recent Pat DNA Gene Seq 2:214-218.
    • (2008) Recent Pat DNA Gene Seq , vol.2 , pp. 214-218
    • Yang, Y.-F.1    Lyu, P.-C.2
  • 26
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman HG (2003) Antibacterial peptides: basic facts and emerging concepts. J Intern Med 254:197-215.
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 27
    • 33646807759 scopus 로고    scopus 로고
    • Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids
    • Liu YJ, Cheng CS, Lai SM, Hsu MP, Chen CS, Lyu PC (2006) Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids. Proteins 63:777-786.
    • (2006) Proteins , vol.63 , pp. 777-786
    • Liu, Y.J.1    Cheng, C.S.2    Lai, S.M.3    Hsu, M.P.4    Chen, C.S.5    Lyu, P.C.6
  • 28
    • 0037260694 scopus 로고    scopus 로고
    • The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP
    • Lay FT, Schirra HJ, Scanlon MJ, Anderson MA, Craik J (2003) The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP. J Mol Biol 325:175-188.
    • (2003) J Mol Biol , vol.325 , pp. 175-188
    • Lay, F.T.1    Schirra, H.J.2    Scanlon, M.J.3    Anderson, M.A.4    Craik, J.5
  • 29
    • 0033772647 scopus 로고    scopus 로고
    • The active site of drosomycin, a small insect antifungal protein, delineated by comparison with the modeled structure of Rs-AFP2, a plant antifungal protein
    • Landon C, Vovelle F, Sodano P, Pajon A (2000) The active site of drosomycin, a small insect antifungal protein, delineated by comparison with the modeled structure of Rs-AFP2, a plant antifungal protein. J Pept Res 56:231-238.
    • (2000) J Pept Res , vol.56 , pp. 231-238
    • Landon, C.1    Vovelle, F.2    Sodano, P.3    Pajon, A.4
  • 30
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham B, Wells J (1989) High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244:1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.1    Wells, J.2
  • 31
    • 0005876924 scopus 로고
    • Bacteriophage lambda cro mutations: Effects on activity and intracellular degradation
    • Pakula AA, Young VB, Sauer RT (1986) Bacteriophage lambda cro mutations: effects on activity and intracellular degradation. Proc Natl Acad Sci USA 83:8829-8833.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8829-8833
    • Pakula, A.A.1    Young, V.B.2    Sauer, R.T.3
  • 32
    • 44049102957 scopus 로고    scopus 로고
    • Peptide sequence and conformation strongly influence tryptophan fluorescence
    • Alston R, Lasagna M, Grimsley G, Scholtz J, Reinhart G, Pace C (2008) Peptide sequence and conformation strongly influence tryptophan fluorescence. Biophys J 94: 2280-2287.
    • (2008) Biophys J , vol.94 , pp. 2280-2287
    • Alston, R.1    Lasagna, M.2    Grimsley, G.3    Scholtz, J.4    Reinhart, G.5    Pace, C.6
  • 33
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for the chemical denaturation of proteins by urea
    • Bennion BJ, Daggett V (2003) The molecular basis for the chemical denaturation of proteins by urea. Proc Natl Acad Sci USA 100:5142-5147.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 35
    • 1042301044 scopus 로고    scopus 로고
    • Structural basis for the inhibition of mammalian and insect α-amylases by plant protein inhibitors
    • Payan F (2004) Structural basis for the inhibition of mammalian and insect α-amylases by plant protein inhibitors. Biochim Biophys Acta 1696:171-180.
    • (2004) Biochim Biophys Acta , vol.1696 , pp. 171-180
    • Payan, F.1
  • 36
    • 0036164521 scopus 로고    scopus 로고
    • Plant α-amylase inhibitors and their interaction with insect α-amylases: Structure, function and potential for crop protection
    • Franco OL, Rigden DJ, Melo FR, Grossi-de-Sa MF (2002) Plant α-amylase inhibitors and their interaction with insect α-amylases: structure, function and potential for crop protection. Eur J Biochem 269:397-412.
    • (2002) Eur J Biochem , vol.269 , pp. 397-412
    • Franco, O.L.1    Rigden, D.J.2    Melo, F.R.3    Grossi-de-Sa, M.F.4
  • 37
    • 0030784243 scopus 로고    scopus 로고
    • Cleavage of the X-Pro peptide bond by pepsin is specific for the trans isomer
    • Vance JE, LeBlanc DA, London RE (1997) Cleavage of the X-Pro peptide bond by pepsin is specific for the trans isomer. Biochemistry 36:13232-13240.
    • (1997) Biochemistry , vol.36 , pp. 13232-13240
    • Vance, J.E.1    LeBlanc, D.A.2    London, R.E.3
  • 38
    • 0037061559 scopus 로고    scopus 로고
    • A unique approach for high level expression and production of a recombinant cobra neurotoxin in Escherichia coli
    • Wang Y, Jing L, Xu K (2002) A unique approach for high level expression and production of a recombinant cobra neurotoxin in Escherichia coli. J Biotechnol 94: 235-244.
    • (2002) J Biotechnol , vol.94 , pp. 235-244
    • Wang, Y.1    Jing, L.2    Xu, K.3
  • 39
    • 38549150372 scopus 로고    scopus 로고
    • Mutagenesis study of rice nonspecific lipid transfer protein 2 reveals residues that contribute to structure and ligand binding
    • Cheng C-S, Chen M-N, Lai Y-T, Chen T, Lin K-F, Liu Y-J, Lyu P-C (2008) Mutagenesis study of rice nonspecific lipid transfer protein 2 reveals residues that contribute to structure and ligand binding. Proteins 70:695-706.
    • (2008) Proteins , vol.70 , pp. 695-706
    • Cheng, C.-S.1    Chen, M.-N.2    Lai, Y.-T.3    Chen, T.4    Lin, K.-F.5    Liu, Y.-J.6    Lyu, P.-C.7
  • 40
    • 0037144489 scopus 로고    scopus 로고
    • Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa)
    • Samuel D, Liu Y-J, Cheng C-S, Lyu P-C (2002) Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa). J Biol Chem 277: 35267-35273.
    • (2002) J Biol Chem , vol.277 , pp. 35267-35273
    • Samuel, D.1    Liu, Y.-J.2    Cheng, C.-S.3    Lyu, P.-C.4
  • 41
    • 0036290222 scopus 로고    scopus 로고
    • Purification and characterization of a novel 7-kDa non-specific lipid transfer protein-2 from rice (Oryza sativa)
    • Liu Y-J, Samuel D, Lin C-H, Lyu P-C (2002) Purification and characterization of a novel 7-kDa non-specific lipid transfer protein-2 from rice (Oryza sativa). Biochem Biophys Res Commun 294:535-540.
    • (2002) Biochem Biophys Res Commun , vol.294 , pp. 535-540
    • Liu, Y.-J.1    Samuel, D.2    Lin, C.-H.3    Lyu, P.-C.4
  • 43
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8:127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 44
    • 21644488250 scopus 로고    scopus 로고
    • Vector NTI, a balanced all-in-one sequence analysis suite
    • Lu G, Moriyama EN (2004) Vector NTI, a balanced all-in-one sequence analysis suite. Brief Bioinform 5: 378-388.
    • (2004) Brief Bioinform , vol.5 , pp. 378-388
    • Lu, G.1    Moriyama, E.N.2


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