메뉴 건너뛰기




Volumn 43, Issue 1, 2009, Pages 11-19

Use of quantitative 1H NMR chemical shift changes for ligand docking into barnase

Author keywords

Barnase; Complexation induced shift; Crystal packing; Docking; Guanine

Indexed keywords

ADENOSINE; BARNASE; CYTOSINE; GUANINE; GUANOSINE; LIGAND; OLIGODEOXYNUCLEOTIDE;

EID: 57549112574     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-008-9286-7     Document Type: Article
Times cited : (29)

References (23)
  • 1
    • 0026279527 scopus 로고
    • Crystal structure of a barnase-g(GpC) complex at 1.9 resolution
    • Baudet S, Janin J (1991) Crystal structure of a barnase-g(GpC) complex at 1.9 resolution. J Mol Biol 219:123-132
    • (1991) J Mol Biol , vol.219 , pp. 123-132
    • Baudet, S.1    Janin, J.2
  • 2
    • 0028287089 scopus 로고
    • Subsite binding in an RNAse: Structure of a barnase tetranucleotide complex at 1.76 resolution
    • Buckle AM, Fersht AR (1994) Subsite binding in an RNAse: Structure of a barnase tetranucleotide complex at 1.76 resolution. Biochemistry 33:1644-1653
    • (1994) Biochemistry , vol.33 , pp. 1644-1653
    • Buckle, A.M.1    Fersht, A.R.2
  • 3
    • 0026044754 scopus 로고
    • Determination of the 3-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy
    • Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM (1991) Determination of the 3-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy. Biochemistry 30:8697-8701
    • (1991) Biochemistry , vol.30 , pp. 8697-8701
    • Bycroft, M.1    Ludvigsen, S.2    Fersht, A.R.3    Poulsen, F.M.4
  • 5
    • 49449095976 scopus 로고    scopus 로고
    • Influence of conformational flexibility on complexation-induced changes in chemical shift in a neocarzinostatin protein-ligand complex
    • Cioffi M, Hunter CA, Packer MJ (2008b) Influence of conformational flexibility on complexation-induced changes in chemical shift in a neocarzinostatin protein-ligand complex. J Med Chem 51:4488-4495
    • (2008) J Med Chem , vol.51 , pp. 4488-4495
    • Cioffi, M.1    Hunter, C.A.2    Packer, M.J.3
  • 6
    • 0026751045 scopus 로고
    • Barnase has subsites that give rise to large rate enhancements
    • Day AG, Parsonage D, Ebel S, Brown T, Fersht AR (1992) Barnase has subsites that give rise to large rate enhancements. Biochemistry 31:6390-6395
    • (1992) Biochemistry , vol.31 , pp. 6390-6395
    • Day, A.G.1    Parsonage, D.2    Ebel, S.3    Brown, T.4    Fersht, A.R.5
  • 7
    • 0041319073 scopus 로고    scopus 로고
    • Filtering and selection of structural models: Combining docking and NMR
    • Dobrodumov A, Gronenborn AM (2003) Filtering and selection of structural models: Combining docking and NMR. Proteins: Struct Funct Genet 53:18-32
    • (2003) Proteins: Struct Funct Genet , vol.53 , pp. 18-32
    • Dobrodumov, A.1    Gronenborn, A.M.2
  • 8
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C, Boelens R, Bonvin A (2003) HADDOCK: A protein-protein docking approach based on biochemical or biophysical information. J Am Chem Soc 125:1731-1737
    • (2003) J Am Chem Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.3
  • 9
    • 0032976814 scopus 로고    scopus 로고
    • 1 H NMR chemical shift for supramolecular structure determination
    • 1 H NMR chemical shift for supramolecular structure determination. Chem Eur J 5:1891-1897
    • (1999) Chem Eur J , vol.5 , pp. 1891-1897
    • Hunter, C.A.1    Packer, M.J.2
  • 10
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267:727-748
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 13
    • 0037009985 scopus 로고    scopus 로고
    • Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations
    • McCoy MA, Wyss DF (2002) Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations. J Am Chem Soc 124:11758-11763
    • (2002) J Am Chem Soc , vol.124 , pp. 11758-11763
    • McCoy, M.A.1    Wyss, D.F.2
  • 14
    • 0027520474 scopus 로고
    • Structure and dynamics of barnase complexed with 3′-GMP studied by NMR spectroscopy
    • Meiering EM, Bycroft M, Lubienski MJ, Fersht AR (1993) Structure and dynamics of barnase complexed with 3′-GMP studied by NMR spectroscopy. Biochemistry 32:10975-10987
    • (1993) Biochemistry , vol.32 , pp. 10975-10987
    • Meiering, E.M.1    Bycroft, M.2    Lubienski, M.J.3    Fersht, A.R.4
  • 16
    • 0034808070 scopus 로고    scopus 로고
    • A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data
    • Morelli XJ, Palma PN, Guerlesquin F, Rigby AC (2001) A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data. Protein Sci 10:2131-2137
    • (2001) Protein Sci , vol.10 , pp. 2131-2137
    • Morelli, X.J.1    Palma, P.N.2    Guerlesquin, F.3    Rigby, A.C.4
  • 17
    • 0024501923 scopus 로고
    • Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis
    • Mossakowska DE, Nyberg K, Fersht AR (1989) Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis. Biochemistry 28:3843-3850
    • (1989) Biochemistry , vol.28 , pp. 3843-3850
    • Mossakowska, D.E.1    Nyberg, K.2    Fersht, A.R.3
  • 19
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane-protein complexes in enzymatically active form
    • Schägger H, von Jägow G (1991) Blue native electrophoresis for isolation of membrane-protein complexes in enzymatically active form. Anal Biochem 199:223-231
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    von Jägow, G.2
  • 21
    • 40149093773 scopus 로고    scopus 로고
    • Rapid protein-ligand costructures using chemical shift perturbations
    • Stark J, Powers R (2008) Rapid protein-ligand costructures using chemical shift perturbations. J Am Chem Soc 130:535-545
    • (2008) J Am Chem Soc , vol.130 , pp. 535-545
    • Stark, J.1    Powers, R.2
  • 22
    • 12544256528 scopus 로고    scopus 로고
    • Data-driven docking for the study of biomolecular complexes
    • van Dijk ADJ, Boelens R, Bonvin AMJJ (2005) Data-driven docking for the study of biomolecular complexes. FEBS J 272:293-312
    • (2005) FEBS J , vol.272 , pp. 293-312
    • van Dijk, A.D.J.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 23
    • 0030255292 scopus 로고    scopus 로고
    • Extended electron distributions applied to the molecular mechanics of some intermolecular interactions. 2. Organic complexes
    • Vinter JG (1996) Extended electron distributions applied to the molecular mechanics of some intermolecular interactions. 2. Organic complexes. J Comp Aided Mol Des 10:417-426
    • (1996) J Comp Aided Mol Des , vol.10 , pp. 417-426
    • Vinter, J.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.