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Volumn 52, Issue 2, 2003, Pages 263-271

The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative

Author keywords

Domain swapping; Protein ligand interaction; Ribonuclease; Three dimensional structure; X ray analysis

Indexed keywords

DIMER; HISTIDINE DERIVATIVE; LIGAND; MONOMER; NUCLEOTIDE; RIBONUCLEASE;

EID: 0038675533     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10407     Document Type: Article
Times cited : (18)

References (51)
  • 1
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines RT. Ribonuclease A. Chem Rev 1998;98:1045-1065.
    • (1998) Chem Rev , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 3
    • 0035185392 scopus 로고    scopus 로고
    • Prevention of human prostate tumor metastasis in athymic mice by antisense targeting of human angiogenin
    • Olson KA, Byers HR, Key ME, Fett JW. Prevention of human prostate tumor metastasis in athymic mice by antisense targeting of human angiogenin. Clin Cancer Res 2001;7:3598-3605.
    • (2001) Clin Cancer Res , vol.7 , pp. 3598-3605
    • Olson, K.A.1    Byers, H.R.2    Key, M.E.3    Fett, J.W.4
  • 4
    • 0036137925 scopus 로고    scopus 로고
    • Phase II trial of a single weekly intravenous dose of ranpirnase in patients with unresectable malignant mesothelioma
    • Mikulski SM, Costanzi JJ, Vogelzang NJ, McCachren S, Taub RN, Chun H, et al. Phase II trial of a single weekly intravenous dose of ranpirnase in patients with unresectable malignant mesothelioma. J Clin Oncol 2002;20:274-281.
    • (2002) J Clin Oncol , vol.20 , pp. 274-281
    • Mikulski, S.M.1    Costanzi, J.J.2    Vogelzang, N.J.3    McCachren, S.4    Taub, R.N.5    Chun, H.6
  • 5
    • 0035018435 scopus 로고    scopus 로고
    • Cancer chemotherapy - Ribonucleases to the rescue
    • Leland PA, Raines RT. Cancer chemotherapy - ribonucleases to the rescue. Chem Biol 2001;8:405-413.
    • (2001) Chem Biol , vol.8 , pp. 405-413
    • Leland, P.A.1    Raines, R.T.2
  • 6
    • 0002849738 scopus 로고    scopus 로고
    • Seminal ribonuclease: The importance of diversity
    • Riordan JF, D'Alessio G, editors. New York: Academic Press
    • D'Alessio G, Di Donato A, Mazzarella L, Piccoli R. Seminal ribonuclease: The importance of diversity. In: Riordan JF, D'Alessio G, editors. Ribonucleases: Structure and function. New York: Academic Press; 1997. p 383-423.
    • (1997) Ribonucleases: Structure and Function , pp. 383-423
    • D'Alessio, G.1    Di Donato, A.2    Mazzarella, L.3    Piccoli, R.4
  • 7
    • 0034817216 scopus 로고    scopus 로고
    • Seminal ribonuclease: Preparation of natural and recombinant enzyme, quaternary isoforms, isoenzymes, monomeric forms: Assay for selective cytotoxicity of the enzyme
    • D'Alessio G, Di Donato A, Piccoli R, Russo N. Seminal ribonuclease: Preparation of natural and recombinant enzyme, quaternary isoforms, isoenzymes, monomeric forms: Assay for selective cytotoxicity of the enzyme. Method Enzymol 2001;341:248-263.
    • (2001) Method Enzymol , vol.341 , pp. 248-263
    • D'Alessio, G.1    Di Donato, A.2    Piccoli, R.3    Russo, N.4
  • 9
    • 0029041305 scopus 로고
    • Swapping structural determinants of ribonucleases: An energetic analysis of the hinge peptide 16-22
    • Mazzarella L, Vitagliano L, Zagari A. Swapping structural determinants of ribonucleases: An energetic analysis of the hinge peptide 16-22. Proc Natl Acad Sci U S A 1995;92:3799-3803.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3799-3803
    • Mazzarella, L.1    Vitagliano, L.2    Zagari, A.3
  • 11
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger MP, Bennett MJ, Eisenberg D. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly. Adv Protein Chem 1997;50:61-122.
    • (1997) Adv Protein Chem , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 12
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu Y, Eisenberg D. 3D domain swapping: As domains continue to swap. Protein Sci 2002;11:1285-1299.
    • (2002) Protein Sci , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 13
    • 0034802585 scopus 로고    scopus 로고
    • Structural properties of trimers and tetramers of ribonuclease A
    • Nenci A, Gotte G, Bertoldi M, Libonati M. Structural properties of trimers and tetramers of ribonuclease A. Protein Sci 2001;10:2017-2027.
    • (2001) Protein Sci , vol.10 , pp. 2017-2027
    • Nenci, A.1    Gotte, G.2    Bertoldi, M.3    Libonati, M.4
  • 14
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth RA, Giannini S, Higgins LD, Conroy MJ, Hounslow AM, Jerala R, Craven CJ, Waltho JP. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J 2001;20:4774-4781.
    • (2001) EMBO J , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6    Craven, C.J.7    Waltho, J.P.8
  • 15
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • Liu Y, Gotte G, Libonati M, Eisenberg D. A domain-swapped RNase A dimer with implications for amyloid formation. Nat Struct Biol 2001;8:211-214.
    • (2001) Nat Struct Biol , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 16
    • 0016735942 scopus 로고
    • Dissociation of bovine seminal ribonuclease into catalytically active monomers by selective reduction and alkylation of the intersubunit disulfide bridges
    • D'Alessio G, Malorni MC, Parente A. Dissociation of bovine seminal ribonuclease into catalytically active monomers by selective reduction and alkylation of the intersubunit disulfide bridges. Biochemistry 1975;14:1116-1122.
    • (1975) Biochemistry , vol.14 , pp. 1116-1122
    • D'Alessio, G.1    Malorni, M.C.2    Parente, A.3
  • 18
    • 0030711635 scopus 로고    scopus 로고
    • From ribonuclease A toward bovine seminal ribonuclease: A step by step thermodynamic analysis
    • Catanzano F, Graziano G, Cafaro V, D'Alessio G, Di Donato A, Barone G. From ribonuclease A toward bovine seminal ribonuclease: A step by step thermodynamic analysis. Biochemistry 1997;36:14403-14408.
    • (1997) Biochemistry , vol.36 , pp. 14403-14408
    • Catanzano, F.1    Graziano, G.2    Cafaro, V.3    D'Alessio, G.4    Di Donato, A.5    Barone, G.6
  • 20
    • 0017612944 scopus 로고
    • Monomeric selectively S-alkylated derivatives of seminal ribonuclease: Preparation and properties
    • Parente A, Albanesi D, Garzillo AM, D'Alessio G. Monomeric selectively S-alkylated derivatives of seminal ribonuclease: Preparation and properties. Ital J Biochem 1977;26:451-466.
    • (1977) Ital J Biochem , vol.26 , pp. 451-466
    • Parente, A.1    Albanesi, D.2    Garzillo, A.M.3    D'Alessio, G.4
  • 21
    • 84872631302 scopus 로고
    • A spectrophotometric method for the measurement of ribonuclease activity
    • Kunitz M. A spectrophotometric method for the measurement of ribonuclease activity. J Biol Chem 1946;164:563-568.
    • (1946) J Biol Chem , vol.164 , pp. 563-568
    • Kunitz, M.1
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 1997;276:307-326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • Navaza J, Saludjian P. AMoRe: An automated molecular replacement program package. Method Enzymol 1997;276:581-594.
    • (1997) Method Enzymol , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 25
    • 0003769049 scopus 로고    scopus 로고
    • New Haven, CT: Department of Molecular Biophysics and Biochemistry, Yale University
    • Brunger AT. X-PLOR version 3.8. New Haven, CT: Department of Molecular Biophysics and Biochemistry, Yale University; 1996.
    • (1996) X-PLOR Version 3.8
    • Brunger, A.T.1
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;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
  • 27
  • 28
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Bailey S. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 1994;50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and conturing of electron-density maps
    • Esnouf RM. Further additions to MolScript version 1.4, including reading and conturing of electron-density maps. Acta Crystallogr D 1999;55:938-940.
    • (1999) Acta Crystallogr D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 31
    • 0032454903 scopus 로고    scopus 로고
    • Binding ofa substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2′,5′)adenosine
    • Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L. Binding ofa substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2′,5′)adenosine. Protein Sci 1998;7:1691-1699.
    • (1998) Protein Sci , vol.7 , pp. 1691-1699
    • Vitagliano, L.1    Adinolfi, S.2    Riccio, A.3    Sica, F.4    Zagari, A.5    Mazzarella, L.6
  • 32
    • 0032714439 scopus 로고    scopus 로고
    • A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease
    • Vitagliano L, Adinolfi S, Sica F, Merlino A, Zagari A, Mazzarella L. A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease. J Mol Biol 1999;293:569-577.
    • (1999) J Mol Biol , vol.293 , pp. 569-577
    • Vitagliano, L.1    Adinolfi, S.2    Sica, F.3    Merlino, A.4    Zagari, A.5    Mazzarella, L.6
  • 33
    • 0034644763 scopus 로고    scopus 로고
    • Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases
    • Pous J, Canals A, Terzyan SS, Guasch A, Benito A, Ribo M, Vilanova M, Coll M. Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases. J Mol Biol 2000;303:49-60.
    • (2000) J Mol Biol , vol.303 , pp. 49-60
    • Pous, J.1    Canals, A.2    Terzyan, S.S.3    Guasch, A.4    Benito, A.5    Ribo, M.6    Vilanova, M.7    Coll, M.8
  • 37
    • 0023631047 scopus 로고
    • Ribonuclease structure and catalysis: Crystal structure of sulfate-free native ribonuclease A at 1.5-Å resolution
    • Campbell RL, Petsko GA. Ribonuclease structure and catalysis: Crystal structure of sulfate-free native ribonuclease A at 1.5-Å resolution. Biochemistry 1987;26:8579-8584.
    • (1987) Biochemistry , vol.26 , pp. 8579-8584
    • Campbell, R.L.1    Petsko, G.A.2
  • 39
    • 0001709899 scopus 로고
    • Ribonuclease-A: Least-squares refinement of the structure at 1.45 Å resolution
    • Borkakoti N, Moss DS, Palmer RA. Ribonuclease-A: Least-squares refinement of the structure at 1.45 Å resolution. Acta Crystallogr B 1982;38:2210-2217.
    • (1982) Acta Crystallogr B , vol.38 , pp. 2210-2217
    • Borkakoti, N.1    Moss, D.S.2    Palmer, R.A.3
  • 40
    • 0028564999 scopus 로고
    • The structures of RNase A complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules
    • Zegers I, Maes D, Dao-Thi MH, Poortmans F, Palmer R, Wyns L. The structures of RNase A complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules. Protein Sci 1994;3:2322-2339.
    • (1994) Protein Sci , vol.3 , pp. 2322-2339
    • Zegers, I.1    Maes, D.2    Dao-Thi, M.H.3    Poortmans, F.4    Palmer, R.5    Wyns, L.6
  • 41
    • 0028322323 scopus 로고
    • The occupancy of two distinct conformations by active-site histidine-119 in crystals of ribonuclease is modulated by pH
    • de Mel VS, Doscher MS, Martin PD, Edwards BF, The occupancy of two distinct conformations by active-site histidine-119 in crystals of ribonuclease is modulated by pH. FEBS Lett 1994;349:155-160.
    • (1994) FEBS Lett , vol.349 , pp. 155-160
    • De Mel, V.S.1    Doscher, M.S.2    Martin, P.D.3    Edwards, B.F.4
  • 42
    • 0023974058 scopus 로고
    • 1H-NMR investigations of the active-site amino acids in semisynthetic RNase S′ and RNase A
    • 1H-NMR investigations of the active-site amino acids in semisynthetic RNase S′ and RNase A. Eur J Biochem 1988;172:485-497.
    • (1988) Eur J Biochem , vol.172 , pp. 485-497
    • Knoblauch, H.1    Ruterjans, H.2    Bloemhoff, W.3    Kerling, K.E.4
  • 43
    • 0020772531 scopus 로고
    • Active site of RNase: Neutron diffraction study of a complex with uridine vanadate, a transitionstate analog
    • Wlodawer A, Miller M, Sjolin L. Active site of RNase: Neutron diffraction study of a complex with uridine vanadate, a transitionstate analog. Proc Natl Acad Sci U S A 1983;80:3628-3631.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 3628-3631
    • Wlodawer, A.1    Miller, M.2    Sjolin, L.3
  • 44
    • 0032535188 scopus 로고    scopus 로고
    • Coulombic effects of remote subsites on the active site of ribonuclease A
    • Fisher BM, Schultz LW, Raines RT. Coulombic effects of remote subsites on the active site of ribonuclease A. Biochemistry 1998;37:17386-17401.
    • (1998) Biochemistry , vol.37 , pp. 17386-17401
    • Fisher, B.M.1    Schultz, L.W.2    Raines, R.T.3
  • 45
    • 0036137804 scopus 로고    scopus 로고
    • Reversible substrate-induced domain motions in ribonuclease A
    • Vitagliano L, Merlino A, Zagari A, Mazzarella L. Reversible substrate-induced domain motions in ribonuclease A. Proteins 2002;46:97-104.
    • (2002) Proteins , vol.46 , pp. 97-104
    • Vitagliano, L.1    Merlino, A.2    Zagari, A.3    Mazzarella, L.4
  • 46
    • 0000875209 scopus 로고
    • Interconversion and phosphoester hydrolysis of 2′,5′- and 3′,5′-dinucleoside monophosphates: Kinetics and mechanisms
    • Jarvinen P, Oivanen M, Lonnberg H. Interconversion and phosphoester hydrolysis of 2′,5′- and 3′,5′-dinucleoside monophosphates: Kinetics and mechanisms. J Org Chem 1991;56:5396-5401.
    • (1991) J Org Chem , vol.56 , pp. 5396-5401
    • Jarvinen, P.1    Oivanen, M.2    Lonnberg, H.3
  • 47
    • 0001055719 scopus 로고    scopus 로고
    • Kinetics and mechanisms for the cleavage and isomerization of the phosphodiester bonds of RNA by Bronsted acids and bases
    • Oivanen M, Kuusela S, Loennberg H. Kinetics and mechanisms for the cleavage and isomerization of the phosphodiester bonds of RNA by Bronsted acids and bases. Chem Rev 1998;98:961-990.
    • (1998) Chem Rev , vol.98 , pp. 961-990
    • Oivanen, M.1    Kuusela, S.2    Loennberg, H.3
  • 49
    • 0035942348 scopus 로고    scopus 로고
    • Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding
    • Park C, Schultz LW, Raines RT. Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding. Biochemistry 2001;40:4949-4956.
    • (2001) Biochemistry , vol.40 , pp. 4949-4956
    • Park, C.1    Schultz, L.W.2    Raines, R.T.3
  • 50
    • 0023088686 scopus 로고
    • Co-operativity in seminal ribonuclease function: Binding studies
    • Di Donato A, Piccoli R, D'Alessio G. Co-operativity in seminal ribonuclease function: Binding studies. Biochem J 1987;241:435-440.
    • (1987) Biochem J , vol.241 , pp. 435-440
    • Di Donato, A.1    Piccoli, R.2    D'Alessio, G.3


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