메뉴 건너뛰기




Volumn 6, Issue 9, 1998, Pages 1141-1151

Mass spectrometric and thermodynamic studies reveal the role of water molecules in complexes formed between SH2 domains and tyrosyl phosphopeptides

Author keywords

Isothermal titration calorimetry; Mass spectrometry; Phosphopeptides; SH2 domain; Water molecules

Indexed keywords


EID: 0032530724     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00115-4     Document Type: Article
Times cited : (60)

References (28)
  • 1
    • 0028057975 scopus 로고
    • Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors
    • Lam, P.Y.S., et al., & Erickson-Vitanen, S. (1994). Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors. Science 263, 380-384.
    • (1994) Science , vol.263 , pp. 380-384
    • Lam, P.Y.S.1    Erickson-Vitanen, S.2
  • 2
    • 0028360180 scopus 로고
    • Design of inhibitors of glycogen phosphorylase: A study of α- and β-C-Glucosides and 1-thio-β-D-glucose compounds
    • Watson, K.A., et al., & Papageorgiou, A. (1994). Design of inhibitors of glycogen phosphorylase: a study of α- and β-C-Glucosides and 1-thio-β-D-glucose compounds. Biochemistry 33, 5745-5758.
    • (1994) Biochemistry , vol.33 , pp. 5745-5758
    • Watson, K.A.1    Papageorgiou, A.2
  • 3
    • 0028272930 scopus 로고
    • Enthalpy of hydrogen bond formation in a protein-ligand binding reaction
    • Connelly, P.R., et al., & Wilson, K.P. (1994). Enthalpy of hydrogen bond formation in a protein-ligand binding reaction. Proc. Natl Acad. Sci. USA 91, 1964-1968.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1964-1968
    • Connelly, P.R.1    Wilson, K.P.2
  • 4
    • 0029706920 scopus 로고    scopus 로고
    • The effect of water on the association constant and the enthalpy of reaction between lysozyme and the specific antibodies D1.3 and D44.1
    • Goldbaum, F.A., Schwarz, F.P., Eisenstein, E., Cauerhff, A., Mariuzza, R.A. & Poljak, R.J. (1996). The effect of water on the association constant and the enthalpy of reaction between lysozyme and the specific antibodies D1.3 and D44.1. J. Mol. Recogn. 9, 6-12.
    • (1996) J. Mol. Recogn. , vol.9 , pp. 6-12
    • Goldbaum, F.A.1    Schwarz, F.P.2    Eisenstein, E.3    Cauerhff, A.4    Mariuzza, R.A.5    Poljak, R.J.6
  • 5
    • 0030471364 scopus 로고    scopus 로고
    • The role of water in sequence-independent ligand binding by an oligopeptide transporter protein
    • Tame, J.R.H., Sleigh, S.H., Wilkinson, A.J. & Ladbury, J.E. (1996). The role of water in sequence-independent ligand binding by an oligopeptide transporter protein. Nat. Struct. Biol. 3, 998-1001.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 998-1001
    • Tame, J.R.H.1    Sleigh, S.H.2    Wilkinson, A.J.3    Ladbury, J.E.4
  • 6
    • 0029134561 scopus 로고
    • The role of water molecules in the structure-based design of (5-hydroxynorvaline)-2-cyclosporin: Synthesis, biological activity and crystallographic analysis with cyclophilin a
    • Mikol, V., Papageorgiou, C. & Borer, X. (1995). The role of water molecules in the structure-based design of (5-hydroxynorvaline)-2-cyclosporin: synthesis, biological activity and crystallographic analysis with cyclophilin A. J. Med. Chem. 38, 3361-3367.
    • (1995) J. Med. Chem. , vol.38 , pp. 3361-3367
    • Mikol, V.1    Papageorgiou, C.2    Borer, X.3
  • 7
    • 0030466444 scopus 로고    scopus 로고
    • Just add water! the effect of water on the specificity of protein-ligand binding sites and its application to drug design
    • Ladbury, J.E. (1996). Just add water! The effect of water on the specificity of protein-ligand binding sites and its application to drug design. Chem. Biol. 3, 973-980.
    • (1996) Chem. Biol. , vol.3 , pp. 973-980
    • Ladbury, J.E.1
  • 8
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine phosphorylated peptides
    • Waksman, G., et al., & Kuriyan, J. (1992). Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine phosphorylated peptides. Nature 358, 646-653.
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1    Kuriyan, J.2
  • 9
    • 0027409064 scopus 로고
    • Binding of high affinity phosphotyrosyl peptide to the src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S.E., Pant, N., Cowburn, D. & Kuriyan, J. (1993). Binding of high affinity phosphotyrosyl peptide to the src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 10
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S.C. & Eck, M.J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 11
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z., et al., & Cantley, L.C. (1993). SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Cantley, L.C.2
  • 12
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray mass spectrometry
    • Loo, J.A. (1997). Studying noncovalent protein complexes by electrospray mass spectrometry. Mass Spectrom. Rev. 16, 1-23.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 13
    • 0027657256 scopus 로고
    • The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry. Promise, pitfalls and prognosis
    • Smith, R.D. & Light Wahl, K.J. (1993). The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry. Promise, pitfalls and prognosis. Biol. Mass Spectrom. 22, 493-501.
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 493-501
    • Smith, R.D.1    Light Wahl, K.J.2
  • 14
    • 0029450365 scopus 로고
    • Hydration in drug design. 1. Multiple hydrogen-bonding features of water molecules in mediating protein-ligand interactions
    • Poornima, C.S. & Dean, P.M. (1995). Hydration in drug design. 1. Multiple hydrogen-bonding features of water molecules in mediating protein-ligand interactions. J. Comp. Aided Mol. Des. 9, 500-512.
    • (1995) J. Comp. Aided Mol. Des. , vol.9 , pp. 500-512
    • Poornima, C.S.1    Dean, P.M.2
  • 15
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford, P.J. (1985). A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28, 849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 17
    • 0030993172 scopus 로고    scopus 로고
    • c-src SH2 domains: A thermodynamic and structural study
    • c-src SH2 domains: a thermodynamic and structural study. Biochemistry 36, 6283-6293.
    • (1997) Biochemistry , vol.36 , pp. 6283-6293
    • Charifson, P.S.1    Consler, T.G.2
  • 18
    • 0029757456 scopus 로고    scopus 로고
    • Alternative modes of tyrosyl phosphopeptide binding to a Src family SH2 domain: Implications for regulation of tyrosine kinase activity
    • Ladbury, J.E., Hensmann, M., Panayotou, G. & Campbell, I.D. (1996). Alternative modes of tyrosyl phosphopeptide binding to a Src family SH2 domain: implications for regulation of tyrosine kinase activity. Biochemistry 35, 11062-11069.
    • (1996) Biochemistry , vol.35 , pp. 11062-11069
    • Ladbury, J.E.1    Hensmann, M.2    Panayotou, G.3    Campbell, I.D.4
  • 21
    • 0030849715 scopus 로고    scopus 로고
    • Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2
    • McNewmar, C., et al., & Weber, P.C. (1997). Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2. Biochemistry 36, 10006-10014.
    • (1997) Biochemistry , vol.36 , pp. 10006-10014
    • McNewmar, C.1    Weber, P.C.2
  • 23
    • 0028130221 scopus 로고
    • Peptide inhibitors of src SH3-SH2 phosphoprotein interactions
    • Gilmer, T., et al., & Kassel, D. (1994). Peptide inhibitors of src SH3-SH2 phosphoprotein interactions. J. Biol. Chem. 269, 31711-31719.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31711-31719
    • Gilmer, T.1    Kassel, D.2
  • 27
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T. Williston, S., Brandts, J.F. & Lin, L.-N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 28
    • 0030266484 scopus 로고    scopus 로고
    • Sensing the heat: The application of isothermal titration calorimetry to the thermodynamic study of biomolecular interactions
    • Ladbury, J.E, Chowdhry, B.Z. (1996). Sensing the heat: the application of isothermal titration calorimetry to the thermodynamic study of biomolecular interactions. Chem. Biol. 3, 791-801.
    • (1996) Chem. Biol. , vol.3 , pp. 791-801
    • Ladbury, J.E.1    Chowdhry, B.Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.