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Volumn 5, Issue 3, 1996, Pages 468-477

Interlobe communication in multiple calcium-binding site mutants of Drosophila calmodulin

Author keywords

calcium binding proteins; circular dichroism; skeletal muscle myosin light chain kinase; UV difference spectroscopy

Indexed keywords

CALCIUM BINDING PROTEIN; CALMODULIN; MYOSIN LIGHT CHAIN KINASE;

EID: 0029972702     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050308     Document Type: Article
Times cited : (39)

References (30)
  • 1
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu YS, Bugg CE, Cook WJ. 1988. Structure of calmodulin refined at 2.2 Å resolution. J Mol Biol 204:191-204.
    • (1988) J Mol Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 2
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31:5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.N.4    Bax, A.5
  • 3
    • 0028558882 scopus 로고
    • Drug binding to calmodulin: Crystal structure of a calmodulin-trifluoperazine complex
    • Cook WJ, Walter LJ, Walter MR. 1994. Drug binding to calmodulin: Crystal structure of a calmodulin-trifluoperazine complex. Biochemistry 33:15259-15265.
    • (1994) Biochemistry , vol.33 , pp. 15259-15265
    • Cook, W.J.1    Walter, L.J.2    Walter, M.R.3
  • 4
    • 9044223939 scopus 로고
    • Ultraviolet difference spectroscopy - New techniques and applications
    • Donovan JW. 1973. Ultraviolet difference spectroscopy - New techniques and applications. Biochemistry 33:15259-15265.
    • (1973) Biochemistry , vol.33 , pp. 15259-15265
    • Donovan, J.W.1
  • 5
    • 0000603323 scopus 로고
    • Biophysical studies of calmodulin
    • Cheung WY, ed. New York: Academic Press
    • Forsén S, Vogel HJ, Drakenberg T. 1986. Biophysical studies of calmodulin. In: Cheung WY, ed. Calcium and cell function, vol VI. New York: Academic Press, pp 113-157.
    • (1986) Calcium and Cell Function , vol.6 , pp. 113-157
    • Forsén, S.1    Vogel, H.J.2    Drakenberg, T.3
  • 7
    • 0023845141 scopus 로고
    • Comparison of the crystal and solution structures of calmodulin and troponin C
    • Heidorn DB, Trewhella J. 1988. Comparison of the crystal and solution structures of calmodulin and troponin C. Biochemistry 27:909-915.
    • (1988) Biochemistry , vol.27 , pp. 909-915
    • Heidorn, D.B.1    Trewhella, J.2
  • 8
    • 0025996973 scopus 로고
    • 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy
    • 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Biochemistry 30:9216-9228.
    • (1991) Biochemistry , vol.30 , pp. 9216-9228
    • Ikura, M.1    Spera, S.2    Barbato, G.3    Kay, L.E.4    Krinks, M.5    Bax, A.6
  • 9
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein
    • Kretsinger RH, Nockolds CE. 1973. Carp muscle calcium-binding protein. J Biol Chem 248:3313-3326.
    • (1973) J Biol Chem , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 11
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • Linse S, Helmersson A, Forsen S. 1991. Calcium binding to calmodulin and its globular domains. J Biol Chem 266:8050-8054.
    • (1991) J Biol Chem , vol.266 , pp. 8050-8054
    • Linse, S.1    Helmersson, A.2    Forsen, S.3
  • 12
    • 0022558415 scopus 로고
    • 2+ on the secondary and tertiary structure of bovine testis calmodulin. A circular-dichroism study
    • 2+ on the secondary and tertiary structure of bovine testis calmodulin. A circular-dichroism study. Biochem J 238:485-490.
    • (1986) Biochem J , vol.238 , pp. 485-490
    • Martin, S.R.1    Bayley, P.M.2
  • 13
    • 0026530375 scopus 로고
    • Stopped-flow studies of calcium dissociation from caicium-binding-site mutants of Drosophila melanogaster
    • Martin SR, Maune JF, Beckingham K, Bayley PM. 1992. Stopped-flow studies of calcium dissociation from caicium-binding-site mutants of Drosophila melanogaster Eur J Biochem 205:1107-1114.
    • (1992) Eur J Biochem , vol.205 , pp. 1107-1114
    • Martin, S.R.1    Maune, J.F.2    Beckingham, K.3    Bayley, P.M.4
  • 17
    • 0027160187 scopus 로고
    • Calcium binding site mutants of calmodulin adopt abnormal conformations in complexes with model target peptides
    • Mukherjea P, Beckingham K. 1993. Calcium binding site mutants of calmodulin adopt abnormal conformations in complexes with model target peptides. Biochem Mol Biol Int 29:555-563.
    • (1993) Biochem Mol Biol Int , vol.29 , pp. 555-563
    • Mukherjea, P.1    Beckingham, K.2
  • 19
    • 0017804062 scopus 로고
    • Conformation-dependent nitration of the protein activator of cyclic adenosine 3′,5′-monophosphate phosphodiesterase
    • Richman PG, Klee CB. 1978. Conformation-dependent nitration of the protein activator of cyclic adenosine 3′,5′-monophosphate phosphodiesterase. Biochemistry 17:928-935.
    • (1978) Biochemistry , vol.17 , pp. 928-935
    • Richman, P.G.1    Klee, C.B.2
  • 20
    • 0018801017 scopus 로고
    • 2+ of tyrosyl residue 138 of calmodulin
    • 2+ of tyrosyl residue 138 of calmodulin. J Biol Chem 254:5372-5376.
    • (1979) J Biol Chem , vol.254 , pp. 5372-5376
    • Richman, P.G.1    Klee, C.B.2
  • 21
    • 0019319097 scopus 로고
    • Calcium- and magnesium-dependent conformational states of calmodulin as determined by nuclear magnetic resonance
    • Seamon KB. 1980. Calcium- and magnesium-dependent conformational states of calmodulin as determined by nuclear magnetic resonance. Biochemistry 19:207-215.
    • (1980) Biochemistry , vol.19 , pp. 207-215
    • Seamon, K.B.1
  • 22
    • 0022429037 scopus 로고
    • Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering
    • Seaton BA, Head JF, Engelman DM, Richards FM. 1985. Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering. Biochemistry 24:6740-6743.
    • (1985) Biochemistry , vol.24 , pp. 6740-6743
    • Seaton, B.A.1    Head, J.F.2    Engelman, D.M.3    Richards, F.M.4
  • 24
    • 0027080159 scopus 로고
    • A series of point mutations reveal interactions between the calcium-binding sites of calmodulin
    • Starovasnik MA, Su DR, Beckingham K, Klevit RE. 1992. A series of point mutations reveal interactions between the calcium-binding sites of calmodulin. Protein Sci 1:245-253.
    • (1992) Protein Sci , vol.1 , pp. 245-253
    • Starovasnik, M.A.1    Su, D.R.2    Beckingham, K.3    Klevit, R.E.4
  • 25
    • 0023900654 scopus 로고
    • Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C
    • Strynadka NCJ, James MNG. 1988. Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C. Proteins Struct Fund Genet 3:1-17.
    • (1988) Proteins Struct Fund Genet , vol.3 , pp. 1-17
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 26
    • 0002752973 scopus 로고
    • Improved media for growing plasmid and cosmid clones
    • Tartof KD, Hobbs CA. 1987. Improved media for growing plasmid and cosmid clones. Bethesda Res Labs Focus 9:12-17.
    • (1987) Bethesda Res Labs Focus , vol.9 , pp. 12-17
    • Tartof, K.D.1    Hobbs, C.A.2
  • 27
    • 0025719432 scopus 로고
    • Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2 Å resolution
    • Taylor DA, Sack JS, Maune JF, Beckingham K, Quiocho FA. 1991. Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2 Å resolution. J Biol Chem 266:21375-21380.
    • (1991) J Biol Chem , vol.266 , pp. 21375-21380
    • Taylor, D.A.1    Sack, J.S.2    Maune, J.F.3    Beckingham, K.4    Quiocho, F.A.5
  • 28
    • 0026536393 scopus 로고
    • Effects of calcium binding on the internal dynamic properties of bovine brain calmodulin, studied by NMR and optical spectroscopy
    • Törok K, Lane AN, Martin SR, Janot JM, Bayley PM. 1992. Effects of calcium binding on the internal dynamic properties of bovine brain calmodulin, studied by NMR and optical spectroscopy. Biochemistry 31: 3452-3462.
    • (1992) Biochemistry , vol.31 , pp. 3452-3462
    • Törok, K.1    Lane, A.N.2    Martin, S.R.3    Janot, J.M.4    Bayley, P.M.5
  • 29
    • 0025748548 scopus 로고
    • Three amino acid substitutions in domain-1 of calmodulin prevent the activation of chicken smooth muscle myosin light chain kinase
    • VanBerkum MRA, Means AR. 1991. Three amino acid substitutions in domain-1 of calmodulin prevent the activation of chicken smooth muscle myosin light chain kinase. J Biol Chem 266:21488-21495.
    • (1991) J Biol Chem , vol.266 , pp. 21488-21495
    • VanBerkum, M.R.A.1    Means, A.R.2
  • 30
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang M, Tanaka T, Ikura M. 1995. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct Biol 2:758-767.
    • (1995) Nature Struct Biol , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.