메뉴 건너뛰기




Volumn 256, Issue 2, 1996, Pages 228-234

Valence screening of water in protein crystals reveals potential Na+ binding sites

Author keywords

Computational biology; Lysozyme; Molecular recognition; Monovalent cations; Thrombin; Water

Indexed keywords

CALCIUM ION; DEOXYRIBONUCLEASE I; ENOLASE; LITHIUM ION; LYSOZYME; MAGNESIUM ION; OXYGEN; PHOSPHOLIPASE A2; POTASSIUM ION; PROTEINASE; RUBIDIUM ION; RUBREDOXIN; SODIUM ION; THROMBIN; WATER;

EID: 0029926326     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0081     Document Type: Editorial
Times cited : (189)

References (25)
  • 1
    • 0028084791 scopus 로고
    • Molecular recognition by thrombin: Role of the slow → fast transition, site-specific ion binding energetics and thermodynamic mapping of structural components
    • Ayala, Y. & Di Cera, E. (1994). Molecular recognition by thrombin: role of the slow → fast transition, site-specific ion binding energetics and thermodynamic mapping of structural components. J. Mol. Biol. 235, 733-746.
    • (1994) J. Mol. Biol. , vol.235 , pp. 733-746
    • Ayala, Y.1    Di Cera, E.2
  • 2
    • 0028950817 scopus 로고
    • Characterizing the microenvironment surrounding protein sites
    • Bagley, S. C. & Altman, R. B. (1995). Characterizing the microenvironment surrounding protein sites. Protein Sci. 4, 622-635.
    • (1995) Protein Sci. , vol.4 , pp. 622-635
    • Bagley, S.C.1    Altman, R.B.2
  • 3
    • 0021095481 scopus 로고
    • X-ray studies of water in crystals of lysozyme
    • Blake, C. C. F., Pulford, W. C. A. & Artymiuk, P. J. (1983). X-ray studies of water in crystals of lysozyme. J. Mol. Biol. 167, 693-723.
    • (1983) J. Mol. Biol. , vol.167 , pp. 693-723
    • Blake, C.C.F.1    Pulford, W.C.A.2    Artymiuk, P.J.3
  • 4
    • 84872498969 scopus 로고
    • Chemical and steric constraints in inorganic solids
    • Brown, I. D. (1992). Chemical and steric constraints in inorganic solids. Acta Crystallog. sect. B, 48, 553-572.
    • (1992) Acta Crystallog. Sect. B , vol.48 , pp. 553-572
    • Brown, I.D.1
  • 5
    • 0025179135 scopus 로고
    • Electronegativity and Lewis acid strength
    • Brown, I. D. & Skowron, A. (1990). Electronegativity and Lewis acid strength. J. Am. Chem. Soc. 112, 3401-3403.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3401-3403
    • Brown, I.D.1    Skowron, A.2
  • 6
    • 0000020840 scopus 로고
    • Empirical parameters for calculating cation-oxygen bond valence
    • Brown, I. D. & Wu, K. K. (1976). Empirical parameters for calculating cation-oxygen bond valence. Acta Crystallog. sect. B, 32, 1957-1959.
    • (1976) Acta Crystallog. Sect. B , vol.32 , pp. 1957-1959
    • Brown, I.D.1    Wu, K.K.2
  • 7
    • 0029014036 scopus 로고
    • An allosteric switch controls the procoagulant and anticoagulant activities of thrombin
    • Dang, Q. D., Vindigni, A. & Di Cera, E. (1995). An allosteric switch controls the procoagulant and anticoagulant activities of thrombin. Proc. Natl Acad. Sci. USA, 92, 5977-5981.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5977-5981
    • Dang, Q.D.1    Vindigni, A.2    Di Cera, E.3
  • 9
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J. P. (1991). Structural aspects of metal liganding to functional groups in proteins. Advan. Protein Chem. 42, 1-75.
    • (1991) Advan. Protein Chem. , vol.42 , pp. 1-75
    • Glusker, J.P.1
  • 10
    • 0028033726 scopus 로고
    • An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase
    • Hohenester, E., Keller, J. W. & Jansonius, J. N. (1994). An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase. Biochemistry, 33, 13561-13570.
    • (1994) Biochemistry , vol.33 , pp. 13561-13570
    • Hohenester, E.1    Keller, J.W.2    Jansonius, J.N.3
  • 12
    • 0028102703 scopus 로고
    • Bases defining an ammonium and magnesium ion-dependent tertiary structure within the large subunit ribosomal RNA
    • Lu, M. & Draper, D. E. (1994). Bases defining an ammonium and magnesium ion-dependent tertiary structure within the large subunit ribosomal RNA. J. Mol. Biol. 244, 572-585.
    • (1994) J. Mol. Biol. , vol.244 , pp. 572-585
    • Lu, M.1    Draper, D.E.2
  • 14
    • 0028897490 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity
    • O'Brien, M. C. & McKay, D. B. (1995). How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity. J. Biol. Chem. 270, 2247-2250.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2247-2250
    • O'Brien, M.C.1    McKay, D.B.2
  • 15
    • 0017802964 scopus 로고
    • The effect of metal ions on the amidolytic activity of human factor Xa (activated Stuart-Prower factor)
    • Orthner, C. L. & Kosow, D. P. (1978). The effect of metal ions on the amidolytic activity of human factor Xa (activated Stuart-Prower factor). Arch. Biochem. Biophys. 185, 400-406.
    • (1978) Arch. Biochem. Biophys. , vol.185 , pp. 400-406
    • Orthner, C.L.1    Kosow, D.P.2
  • 16
    • 0019255615 scopus 로고
    • Evidence that human α-thrombin is a monovalent cation-activated enzyme
    • Orthner, C. L. & Kosow, D. P. (1980). Evidence that human α-thrombin is a monovalent cation-activated enzyme. Arch. Biochem. Biophys. 202, 63-75.
    • (1980) Arch. Biochem. Biophys. , vol.202 , pp. 63-75
    • Orthner, C.L.1    Kosow, D.P.2
  • 17
    • 0028297873 scopus 로고
    • Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. Escherichia coli SSB protein-single stranded nucleic acid interactions
    • Overman, L. B. & Lohman, T. M. (1994). Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. Escherichia coli SSB protein-single stranded nucleic acid interactions. J. Mol. Biol. 236, 165-178.
    • (1994) J. Mol. Biol. , vol.236 , pp. 165-178
    • Overman, L.B.1    Lohman, T.M.2
  • 19
    • 0019324165 scopus 로고
    • Stimulation of the amidase and esterase activity of activated bovine plasma protein C by monovalent cations
    • Steiner, S. A., Amphlett, G. N. & Castellino, F. J. (1980). Stimulation of the amidase and esterase activity of activated bovine plasma protein C by monovalent cations. Biochem. Biophys. Res. Commun. 94, 340-347.
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 340-347
    • Steiner, S.A.1    Amphlett, G.N.2    Castellino, F.J.3
  • 20
    • 0014947813 scopus 로고
    • Enzymes activated by monovalent cations
    • Suelter, C. H. (1970). Enzymes activated by monovalent cations. Science, 168, 789-795.
    • (1970) Science , vol.168 , pp. 789-795
    • Suelter, C.H.1
  • 21
    • 0027182377 scopus 로고
    • Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites
    • Toney, M. D., Hohenester, E., Cowan, S. W. & Jansonius, J. N. (1993). Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science, 261, 756-759.
    • (1993) Science , vol.261 , pp. 756-759
    • Toney, M.D.1    Hohenester, E.2    Cowan, S.W.3    Jansonius, J.N.4
  • 23
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks, S. M. & McKay, D. B. (1995). How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270, 2251-2257.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 24
    • 0029117821 scopus 로고
    • Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex
    • Woehl, E. U. & Dunn, M. F. (1995). Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex. Biochemistry, 34, 9466-9476.
    • (1995) Biochemistry , vol.34 , pp. 9466-9476
    • Woehl, E.U.1    Dunn, M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.