메뉴 건너뛰기




Volumn 272, Issue 3, 2005, Pages 744-755

Binding of non-natural 3′-nucleotides to ribonuclease A

Author keywords

2 fluoro 2 deoxynucleotide; Arabinonucleotide; Enzyme inhibitor; Ribonuclease; X ray crystallography

Indexed keywords

2' FLUORO 2' DEOXYURIDINE 3' PHOSPHATE; ARABINONUCLEOTIDE; ARABINOURIDINE 3' PHOSPHATE; HYDROXYL GROUP; NUCLEIC ACID BASE; RIBONUCLEASE A; UNCLASSIFIED DRUG; URACIL;

EID: 13444266054     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2004.04511.x     Document Type: Article
Times cited : (15)

References (47)
  • 1
    • 0031697202 scopus 로고    scopus 로고
    • The ribonuclease A superfamily: General discussion
    • Beintema JJ & Kleineidam RG (1998) The ribonuclease A superfamily: General discussion. Cell Mol Life Sci 54, 825-842.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 825-842
    • Beintema, J.J.1    Kleineidam, R.G.2
  • 4
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines RT (1998) Ribonuclease A. Chem Rev 98, 1045-1065.
    • (1998) Chem Rev , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 5
    • 0024522906 scopus 로고
    • Role of lysines in human angiogenin: Chemical modification and site-directed mutagenesis
    • Shapiro R, Fox EA & Riordan JF (1989) Role of lysines in human angiogenin: Chemical modification and site-directed mutagenesis. Biochemistry 28, 1726-1732.
    • (1989) Biochemistry , vol.28 , pp. 1726-1732
    • Shapiro, R.1    Fox, E.A.2    Riordan, J.F.3
  • 6
    • 0024435026 scopus 로고
    • Site-directed mutagenesis of histidine-13 and histidine-114 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis
    • Shapiro R & Vallee BL (1989) Site-directed mutagenesis of histidine-13 and histidine-114 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis. Biochemistry 28, 7401-7408.
    • (1989) Biochemistry , vol.28 , pp. 7401-7408
    • Shapiro, R.1    Vallee, B.L.2
  • 8
    • 0033543235 scopus 로고    scopus 로고
    • Toward rational design of ribonuclease inhibitors: High resolution crystal structure of a ribonuclease A complex with a potent 3′,5′- pyrophosphate-linked dinucleotide inhibitor
    • Leonidas DD, Shapiro R, Irons LI, Russo N & Acharya KR (1999) Toward rational design of ribonuclease inhibitors: High resolution crystal structure of a ribonuclease A complex with a potent 3′,5′-pyrophosphate-linked dinucleotide inhibitor. Biochemistry 38, 10287-10297.
    • (1999) Biochemistry , vol.38 , pp. 10287-10297
    • Leonidas, D.D.1    Shapiro, R.2    Irons, L.I.3    Russo, N.4    Acharya, K.R.5
  • 9
    • 0034803941 scopus 로고    scopus 로고
    • Small molecule inhibitors of RNase A and related enzymes
    • Russo A, Acharya KR & Shapiro R (2001) Small molecule inhibitors of RNase A and related enzymes. Methods Enzymol 341, 629-648.
    • (2001) Methods Enzymol , vol.341 , pp. 629-648
    • Russo, A.1    Acharya, K.R.2    Shapiro, R.3
  • 10
    • 0033591409 scopus 로고    scopus 로고
    • Potent inhibition of mammalian ribonucleases by 3′,5′- pyrophosphate-linked nucleotides
    • Russo N & Shapiro R (1999) Potent inhibition of mammalian ribonucleases by 3′,5′-pyrophosphate-linked nucleotides. J Biol Chem 274, 14902-14908.
    • (1999) J Biol Chem , vol.274 , pp. 14902-14908
    • Russo, N.1    Shapiro, R.2
  • 11
    • 17144442771 scopus 로고    scopus 로고
    • 5′-diphosphoadenosine 3′-phosphate is a potent inhibitor of bovine pancreatic ribonuclease A
    • Russo N, Shapiro R & Vallee BL (1997) 5′-Diphosphoadenosine 3′-phosphate is a potent inhibitor of bovine pancreatic ribonuclease A. Biochem Biophys Res Commun 231, 671-674.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 671-674
    • Russo, N.1    Shapiro, R.2    Vallee, B.L.3
  • 15
    • 0034601629 scopus 로고    scopus 로고
    • A new method for the phosphorylation of nucleosides
    • Taktakishvili M & Nair V (2000) A new method for the phosphorylation of nucleosides. Tetrahedron Lett 41, 7173-7176.
    • (2000) Tetrahedron Lett , vol.41 , pp. 7173-7176
    • Taktakishvili, M.1    Nair, V.2
  • 16
    • 13444266865 scopus 로고
    • The conformations of phosphorylating derivatives of 2′-fluoro- 2′-deoxyuridine in solution
    • Antonov IV, Dudkin SM, Karpeiskii MY & Yakovlev GI (1976) The conformations of phosphorylating derivatives of 2′-fluoro-2′- deoxyuridine in solution. Sov J Bioorg Chem 2, 863-872.
    • (1976) Sov J Bioorg Chem , vol.2 , pp. 863-872
    • Antonov, I.V.1    Dudkin, S.M.2    Karpeiskii, M.Y.3    Yakovlev, G.I.4
  • 17
    • 0005220594 scopus 로고
    • Nucleosides. XVIII. Synthesis of 2′-fluorothymidine, 2′-fluorodeoxyuridine, and other 2′-halogeno-2′- deoxynucleosides
    • Codington JF, Doerr IL & Fox JJ (1964) Nucleosides. XVIII. Synthesis of 2′-fluorothymidine, 2′-fluorodeoxyuridine, and other 2′-halogeno-2′-deoxynucleosides. J Org Chem 29, 558-564.
    • (1964) J Org Chem , vol.29 , pp. 558-564
    • Codington, J.F.1    Doerr, I.L.2    Fox, J.J.3
  • 18
    • 0001129165 scopus 로고
    • A new, convenient and efficient general procedure for the conversion of alcohols into their dibenzyl phosphorotriesters using N,N-diethyl dibenzyl phosphoramidite
    • Perich JW & Johns RB (1987) A new, convenient and efficient general procedure for the conversion of alcohols into their dibenzyl phosphorotriesters using N,N-diethyl dibenzyl phosphoramidite. Tetrahedron Lett 28, 101-102.
    • (1987) Tetrahedron Lett , vol.28 , pp. 101-102
    • Perich, J.W.1    Johns, R.B.2
  • 19
    • 0037018469 scopus 로고    scopus 로고
    • Synthesis of 2-C-methyl-D-erythritol-2,4-cyclopyrophosphate
    • Giner J-L & Ferris WV Jr (2002) Synthesis of 2-C-methyl-D-erythritol- 2,4-cyclopyrophosphate. Org Lett 4, 1225-1226.
    • (2002) Org Lett , vol.4 , pp. 1225-1226
    • Giner, J.-L.1    Ferris Jr., W.V.2
  • 20
    • 0027477934 scopus 로고
    • A new method for the detritylation of alcohols bearing other reducible and acid-hydrolyzable functionalities
    • Krainer E & Naider F (1993) A new method for the detritylation of alcohols bearing other reducible and acid-hydrolyzable functionalities. Tetrahedron Lett 34, 1713-1716.
    • (1993) Tetrahedron Lett , vol.34 , pp. 1713-1716
    • Krainer, E.1    Naider, F.2
  • 21
    • 0030816743 scopus 로고    scopus 로고
    • Arabinonucleotide synthesis by the epoxide route
    • Roussev CD, Simeonov MF & Petkov DD (1997) Arabinonucleotide synthesis by the epoxide route. J Org Chem 62, 5238-5240.
    • (1997) J Org Chem , vol.62 , pp. 5238-5240
    • Roussev, C.D.1    Simeonov, M.F.2    Petkov, D.D.3
  • 22
    • 0343875889 scopus 로고
    • Arabinonucleotides. II. The synthesis of O2,2′-anhydrocytidine 3′-phosphate, a precursor of 1-β-D-arabinosylcytosine
    • Nagyvary J (1969) Arabinonucleotides. II. The synthesis of O2,2′-anhydrocytidine 3′-phosphate, a precursor of 1-β-D-arabinosylcytosine. J Am Chem Soc 91, 5409-5410.
    • (1969) J Am Chem Soc , vol.91 , pp. 5409-5410
    • Nagyvary, J.1
  • 23
    • 0015922102 scopus 로고
    • Inhibition of pancreatic ribonuclease A by arabinonucleotides
    • Pollard DR & Nagyvary J (1973) Inhibition of pancreatic ribonuclease A by arabinonucleotides. Biochemistry 12, 1063-1066.
    • (1973) Biochemistry , vol.12 , pp. 1063-1066
    • Pollard, D.R.1    Nagyvary, J.2
  • 24
    • 0005592113 scopus 로고
    • Nucleosides XXVI. A facile synthesis of 2,2′-anhydro-arabino pyrimidine nucleosides
    • Fox JJ & Wempen I (1965) Nucleosides XXVI. A facile synthesis of 2,2′-anhydro-arabino pyrimidine nucleosides. Tetrahedron Lett 6, 643-646.
    • (1965) Tetrahedron Lett , vol.6 , pp. 643-646
    • Fox, J.J.1    Wempen, I.2
  • 26
    • 0015239608 scopus 로고
    • Kinetic and equilibrium studies on the interaction of ribonuclease A and 2′-deoxyuridine-3′phosphate
    • Walz FG Jr (1971) Kinetic and equilibrium studies on the interaction of ribonuclease A and 2′-deoxyuridine-3′phosphate. Biochemistry 10, 2156-2162.
    • (1971) Biochemistry , vol.10 , pp. 2156-2162
    • Walz Jr., F.G.1
  • 28
    • 0142210123 scopus 로고    scopus 로고
    • High resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors
    • Leonidas DD, Chavali GB, Oikonomakos NG, Chrysina ED, Kosmopoulou MN, Vlassi M, Frankling C & Acharya KR (2003) High resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors. Protein Sci 12, 2559-2574.
    • (2003) Protein Sci , vol.12 , pp. 2559-2574
    • Leonidas, D.D.1    Chavali, G.B.2    Oikonomakos, N.G.3    Chrysina, E.D.4    Kosmopoulou, M.N.5    Vlassi, M.6    Frankling, C.7    Acharya, K.R.8
  • 29
    • 0030917539 scopus 로고    scopus 로고
    • Crystal structures of ribonuclease A complexes with 5′- diphosphoadenosine 3′-phosphate and 5′-diphosphoadenosine 2′-phosphate at 1.7 A resolution
    • Leonidas DD, Shapiro R, Irons LI, Russo N & Acharya KR (1997) Crystal structures of ribonuclease A complexes with 5′-diphosphoadenosine 3′-phosphate and 5′-diphosphoadenosine 2′-phosphate at 1.7 A resolution. Biochemistry 36, 5578-5588.
    • (1997) Biochemistry , vol.36 , pp. 5578-5588
    • Leonidas, D.D.1    Shapiro, R.2    Irons, L.I.3    Russo, N.4    Acharya, K.R.5
  • 30
    • 0031671322 scopus 로고    scopus 로고
    • The contribution of noncatalytic phosphate-binding subsites to the mechanism of bovine pancreatic ribonuclease A
    • Nogués MV, Moussaoui M, Boix E, Vilanova M, Ribo M & Cuchillo CM (1998) The contribution of noncatalytic phosphate-binding subsites to the mechanism of bovine pancreatic ribonuclease A. Cell Mol Life Sci 54, 766-774.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 766-774
    • Nogués, M.V.1    Moussaoui, M.2    Boix, E.3    Vilanova, M.4    Ribo, M.5    Cuchillo, C.M.6
  • 31
    • 0015511563 scopus 로고
    • Conformational analysis of the sugar ring in nucleosides and nucleotides. A new description using the concept of pseudorotation
    • Altona C & Sundaralingam M (1972) Conformational analysis of the sugar ring in nucleosides and nucleotides. A new description using the concept of pseudorotation. J Am Chem Soc 94, 8205-8212.
    • (1972) J Am Chem Soc , vol.94 , pp. 8205-8212
    • Altona, C.1    Sundaralingam, M.2
  • 32
    • 0016634528 scopus 로고
    • Nuclear magnetic resonance studies of 2′- and 3′- ribonucleotide structures in solution
    • Davies DB & Danyluk SS (1975) Nuclear magnetic resonance studies of 2′- and 3′-ribonucleotide structures in solution. Biochemistry 14, 543-554.
    • (1975) Biochemistry , vol.14 , pp. 543-554
    • Davies, D.B.1    Danyluk, S.S.2
  • 33
    • 0019332380 scopus 로고
    • Nucleoside conformation is determined by the electronegativity of the sugar substituent
    • Guschlbauer W & Jankowski K (1980) Nucleoside conformation is determined by the electronegativity of the sugar substituent. Nucleic Acids Res 8, 1421-1433.
    • (1980) Nucleic Acids Res , vol.8 , pp. 1421-1433
    • Guschlbauer, W.1    Jankowski, K.2
  • 34
    • 0003817731 scopus 로고
    • Intramolecular hydrogen bonding in 1-β-D-arabinofuranosylcytosine (Ara-C)
    • Chwang AK & Sundaralingam M (1973) Intramolecular hydrogen bonding in 1-β-D-arabinofuranosylcytosine (Ara-C). Nat New Biol 243, 78-79.
    • (1973) Nat New Biol , vol.243 , pp. 78-79
    • Chwang, A.K.1    Sundaralingam, M.2
  • 35
    • 0033575071 scopus 로고    scopus 로고
    • Effects of C2′-substitution on arabinonucleic acid structure and conformation
    • Venkateswarlu D & Ferguson DM (1999) Effects of C2′- substitution on arabinonucleic acid structure and conformation. J Am Ghent Soc 121, 5609-5610.
    • (1999) J Am Ghent Soc , vol.121 , pp. 5609-5610
    • Venkateswarlu, D.1    Ferguson, D.M.2
  • 36
    • 0034727637 scopus 로고    scopus 로고
    • Excavating an active site: The nucleobase specificity of ribonuclease A
    • Kelemen BR, Schultz LW, Sweeney RY & Raines RT (2000) Excavating an active site: The nucleobase specificity of ribonuclease A. Biochemistry 39, 14487-14494.
    • (2000) Biochemistry , vol.39 , pp. 14487-14494
    • Kelemen, B.R.1    Schultz, L.W.2    Sweeney, R.Y.3    Raines, R.T.4
  • 37
    • 0030590426 scopus 로고    scopus 로고
    • How good is fluorine as a hydrogen bond acceptor?
    • Howard JAK, Hoy VJ, O'Hagan D & Smith GT (1996) How good is fluorine as a hydrogen bond acceptor?. Tetrahedron 52, 12613-12622.
    • (1996) Tetrahedron , vol.52 , pp. 12613-12622
    • Howard, J.A.K.1    Hoy, V.J.2    O'Hagan, D.3    Smith, G.T.4
  • 38
    • 0028275049 scopus 로고
    • Structural determinants of enzymatic processivity
    • delCardayré SB & Raines RT (1994) Structural determinants of enzymatic processivity. Biochemistry 33, 6031-6037.
    • (1994) Biochemistry , vol.33 , pp. 6031-6037
    • DelCardayré, S.B.1    Raines, R.T.2
  • 39
    • 0029091002 scopus 로고
    • A residue to residue hydrogen bond mediates the nucleotide specificity of ribonuclease A
    • delCardayré SB & Raines RT (1995) A residue to residue hydrogen bond mediates the nucleotide specificity of ribonuclease A. J Mol Biol 252, 328-336.
    • (1995) J Mol Biol , vol.252 , pp. 328-336
    • DelCardayré, S.B.1    Raines, R.T.2
  • 40
    • 0034846027 scopus 로고    scopus 로고
    • Properties of arabinonucleic acids (ANA & 2′F-ANA): Implications for the design of antisense therapeutics that invoke RNase H cleavage of RNA
    • Dahma MJ, Noronha AM, Wilds CJ, Trempe JF, Denisov A, Pon RT & Gehring K (2001) Properties of arabinonucleic acids (ANA & 2′F-ANA): Implications for the design of antisense therapeutics that invoke RNase H cleavage of RNA Nucleosides Nucleotides Nucleic Acids 20, 429-440.
    • (2001) Nucleosides Nucleotides Nucleic Acids , vol.20 , pp. 429-440
    • Dahma, M.J.1    Noronha, A.M.2    Wilds, C.J.3    Trempe, J.F.4    Denisov, A.5    Pon, R.T.6    Gehring, K.7
  • 41
    • 0029032586 scopus 로고
    • Engineering ribonuclease A: Production, purification, and characterization of wild-type enzyme and mutants at Gln11
    • delCardayré SB, Ribó M, Yokel EM, Quirk DJ, Rutter WJ & Raines RT (1995) Engineering ribonuclease A: Production, purification, and characterization of wild-type enzyme and mutants at Gln11. Protein Eng 8, 261-273.
    • (1995) Protein Eng , vol.8 , pp. 261-273
    • DelCardayré, S.B.1    Ribó, M.2    Yokel, E.M.3    Quirk, D.J.4    Rutter, W.J.5    Raines, R.T.6
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z & Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW & Kjeldgaard M (1991) Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr A 47, 110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 45
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger AT (1992) Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 46
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • Kleywegt GJ & Jones TA (1998) Databases in protein crystallography. Acta Crystallogr D 54, 1119-1131.
    • (1998) Acta Crystallogr D , vol.54 , pp. 1119-1131
    • Kleywegt, G.J.1    Jones, T.A.2
  • 47
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 15, 132-134.
    • (1997) J Mol Graph Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.