메뉴 건너뛰기




Volumn 85, Issue 7, 1996, Pages 1057-1065

Hydration and DNA recognition by homeodomains

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DNA; HOMEODOMAIN PROTEIN; HYDROGEN; WATER;

EID: 0030604702     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81306-9     Document Type: Article
Times cited : (103)

References (34)
  • 2
    • 0001386993 scopus 로고
    • Hydration water molecules seen by NMR and x-ray crystallography
    • Billeter, M. (1995). Hydration water molecules seen by NMR and x-ray crystallography. Prog. NMR Spectr. 27, 635-645.
    • (1995) Prog. NMR Spectr. , vol.27 , pp. 635-645
    • Billeter, M.1
  • 3
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex
    • Billeter, M., Qian, Y.Q., Otting, G., Müller, M., Gehring, W.J., and Wüthrich, K. (1993). Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex. J. Mol. Biol. 234, 1084-1093.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1084-1093
    • Billeter, M.1    Qian, Y.Q.2    Otting, G.3    Müller, M.4    Gehring, W.J.5    Wüthrich, K.6
  • 4
    • 0028852791 scopus 로고
    • Three-dimensional structure and actions of immunosuppressants and their immunophilins
    • Braun, W., Kallen, J., Mikol, V., Walkinshaw, M.D., and Wüthrich, K. (1995). Three-dimensional structure and actions of immunosuppressants and their immunophilins. FASEB J. 9, 63-72.
    • (1995) FASEB J. , vol.9 , pp. 63-72
    • Braun, W.1    Kallen, J.2    Mikol, V.3    Walkinshaw, M.D.4    Wüthrich, K.5
  • 5
    • 0027304152 scopus 로고
    • Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations
    • Brunne, R.M., Liepinsh, E., Otting, G., Wüthrich, K., and van Gunsteren, W.F. (1993). Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations. J. Mol. Biol. 231, 1040-1048.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1040-1048
    • Brunne, R.M.1    Liepinsh, E.2    Otting, G.3    Wüthrich, K.4    Van Gunsteren, W.F.5
  • 6
    • 0028948786 scopus 로고
    • Protein hydration dynamics in aqueous solution: A comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion
    • Denisov, V.P., and Halle, B. (1995). Protein hydration dynamics in aqueous solution: a comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion. J. Mol. Biol. 245, 682-697.
    • (1995) J. Mol. Biol. , vol.245 , pp. 682-697
    • Denisov, V.P.1    Halle, B.2
  • 7
    • 0000543918 scopus 로고
    • Exchange rates of internal water molecules in proteins measured using pulsed field gradients
    • Dötsch, V., and Wider, G. (1995). Exchange rates of internal water molecules in proteins measured using pulsed field gradients. J. Am. Chem. Soc. 117, 6064-6070.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6064-6070
    • Dötsch, V.1    Wider, G.2
  • 9
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • Dunitz, J.D. (1994). The entropic cost of bound water in crystals and biomolecules. Science 264, 670.
    • (1994) Science , vol.264 , pp. 670
    • Dunitz, J.D.1
  • 10
    • 0000276909 scopus 로고
    • Water structure associated with proteins and its role in crystallization
    • Frey, M. (1994). Water structure associated with proteins and its role in crystallization. Acta Crystallogr. D50, 663-666.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 663-666
    • Frey, M.1
  • 12
    • 0029010368 scopus 로고
    • The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex
    • Gewirth, D.T., and Sigler, P.W. (1995). The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex. Struct. Biol. 2, 386-394.
    • (1995) Struct. Biol. , vol.2 , pp. 386-394
    • Gewirth, D.T.1    Sigler, P.W.2
  • 13
    • 0000088628 scopus 로고
    • Processing of multidimensional NMR data with the software PROSA
    • Güntert, P., Dötsch, V., Wider, G., and Wüthrich, K. (1992). Processing of multidimensional NMR data with the software PROSA. J. Biomol. NMR 2, 619-629.
    • (1992) J. Biomol. NMR , vol.2 , pp. 619-629
    • Güntert, P.1    Dötsch, V.2    Wider, G.3    Wüthrich, K.4
  • 14
    • 0024320441 scopus 로고
    • DNA specificity of the bicoid activation protein is determined by homeodomain recognition helix residue 9
    • Hanes, S.D., and Brent, R. (1989). DNA specificity of the bicoid activation protein is determined by homeodomain recognition helix residue 9. Cell 57, 1275-1283.
    • (1989) Cell , vol.57 , pp. 1275-1283
    • Hanes, S.D.1    Brent, R.2
  • 15
    • 0029595248 scopus 로고
    • Structure of the even-skipped homeodomain complexed to AT-rich DNA: New perspectives on homeodomain specificity
    • Hirsch, J.A., and Aggarwal, A.K. (1995). Structure of the even-skipped homeodomain complexed to AT-rich DNA: new perspectives on homeodomain specificity. EMBO J. 14, 6280-6291.
    • (1995) EMBO J. , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 16
    • 0028097538 scopus 로고
    • Ordered water in macromolecular structure
    • Karplus, P.A., and Faerman, C. (1994). Ordered water in macromolecular structure. Curr. Opin. Struct. Biol. 4, 770-776.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 770-776
    • Karplus, P.A.1    Faerman, C.2
  • 17
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • in press
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 27, in press.
    • (1996) J. Mol. Graph. , vol.27
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 18
    • 0024997404 scopus 로고
    • Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution
    • Otting, G., Qian, Y.Q., Billeter, M., Müller, M., Affolter, M., Gehring, W.J., and Wüthrich, K. (1990). Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO J. 9, 3085-3092.
    • (1990) EMBO J. , vol.9 , pp. 3085-3092
    • Otting, G.1    Qian, Y.Q.2    Billeter, M.3    Müller, M.4    Affolter, M.5    Gehring, W.J.6    Wüthrich, K.7
  • 19
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • Otting, G., Liepinsh, E., and Wüthrich, K. (1991a). Protein hydration in aqueous solution. Science 254, 974-980.
    • (1991) Science , vol.254 , pp. 974-980
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 20
    • 84957316785 scopus 로고
    • Proton exchange with internal water molecules in the protein BPTI in aqueous solution
    • Otting, G., Liepinsh, E., and Wüthrich, K. (1991b). Proton exchange with internal water molecules in the protein BPTI in aqueous solution. J. Am. Chem. Soc. 113, 4363-4364.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4363-4364
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 22
    • 0025155089 scopus 로고
    • The interaction with DNA of wild-type and mutant fushi tarazu homeodomains
    • Corrigendum EMBO J. 11, 382
    • Percival-Smith, A., Müller, M., Affolter, M., and Gehring, W.J. (1990). The interaction with DNA of wild-type and mutant fushi tarazu homeodomains. EMBO J. 9, 3967-3974. Corrigendum EMBO J. 11, 382.
    • (1990) EMBO J. , vol.9 , pp. 3967-3974
    • Percival-Smith, A.1    Müller, M.2    Affolter, M.3    Gehring, W.J.4
  • 23
    • 0000764227 scopus 로고
    • NMR detection of hydration water in the intermolecular interface of a protein-DNA complex
    • Qian, Y.Q., Otting, G., and Wüthrich, K. (1993a). NMR detection of hydration water in the intermolecular interface of a protein-DNA complex. J. Amer. Chem. Soc. 115, 1189-1190.
    • (1993) J. Amer. Chem. Soc. , vol.115 , pp. 1189-1190
    • Qian, Y.Q.1    Otting, G.2    Wüthrich, K.3
  • 25
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J., Ciccotti, G., and Berendsen, H.C.J. (1977). Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comp. Phys. 23, 327-341.
    • (1977) J. Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.1    Ciccotti, G.2    Berendsen, H.C.J.3
  • 26
    • 0028875233 scopus 로고
    • Exploring the role of the solvent in the denaturation of a protein: A molecular dynamics study of the DNA binding domain of the 434 repressor
    • Schiffer, C., Dötsch, V., Wüthrich, K., and van Gunsteren, W.F. (1995). Exploring the role of the solvent in the denaturation of a protein: a molecular dynamics study of the DNA binding domain of the 434 repressor. Biochemistry 34, 15057-15067.
    • (1995) Biochemistry , vol.34 , pp. 15057-15067
    • Schiffer, C.1    Dötsch, V.2    Wüthrich, K.3    Van Gunsteren, W.F.4
  • 27
    • 0024278949 scopus 로고
    • Distribution of water around amino acid residues in proteins
    • Thanki, N., Thornton, J.M., and Goodfellow, J.M. (1988). Distribution of water around amino acid residues in proteins. J. Mol. Biol. 202, 637-657.
    • (1988) J. Mol. Biol. , vol.202 , pp. 637-657
    • Thanki, N.1    Thornton, J.M.2    Goodfellow, J.M.3
  • 28
    • 0024397687 scopus 로고
    • A single amino acid can determine the DNA binding specificity of homeodomain proteins
    • Treisman, J., Gönczy, P., Vashishtha, M., Harris, E., and Desplan, C. (1989). A single amino acid can determine the DNA binding specificity of homeodomain proteins. Cell 59, 553-562.
    • (1989) Cell , vol.59 , pp. 553-562
    • Treisman, J.1    Gönczy, P.2    Vashishtha, M.3    Harris, E.4    Desplan, C.5
  • 29
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S.J, Kollman, P.A., Nguyen, D.T., and Case, D.A. (1986). An all atom force field for simulations of proteins and nucleic acids. J. Comp. Chem. 7, 230-252.
    • (1986) J. Comp. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 30
    • 0029160486 scopus 로고
    • High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA
    • Wilson, D.S., Guenther, B., Desplan, C., and Kuriyan, J. (1995). High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA. Cell 82, 709-719.
    • (1995) Cell , vol.82 , pp. 709-719
    • Wilson, D.S.1    Guenther, B.2    Desplan, C.3    Kuriyan, J.4
  • 32
    • 0027815738 scopus 로고
    • Hydration of biological macromolecules in solution: Surface structure and molecular recognition
    • Wüthrich, K. (1993). Hydration of biological macromolecules in solution: surface structure and molecular recognition. In DNA and Chromosomes, Cold Spring Harbor Symp. Quant. Biol. 58, 149-157.
    • (1993) DNA and Chromosomes, Cold Spring Harbor Symp. Quant. Biol. , vol.58 , pp. 149-157
    • Wüthrich, K.1
  • 34
    • 0028341789 scopus 로고
    • Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme
    • Zhang, X.-J., and Matthews, B.W. (1994). Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme. Protein Sci. 3, 1031-1039.
    • (1994) Protein Sci. , vol.3 , pp. 1031-1039
    • Zhang, X.-J.1    Matthews, B.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.