메뉴 건너뛰기




Volumn 110, Issue 2, 1997, Pages 173-184

Molecular tuning of an EF-hand-like calcium binding loop: Contributions of the coordinating side chain at loop position 3

Author keywords

Calcium signaling; Calmodulin; Ion channels; Metal binding site; Troponin C

Indexed keywords

CALCIUM ION; ION CHANNEL;

EID: 0030872564     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.110.2.173     Document Type: Article
Times cited : (30)

References (59)
  • 2
    • 0028834424 scopus 로고
    • The elemental principles of calcium signaling
    • Rootman, M.D., and M.J. Berridge. 1995. The elemental principles of calcium signaling. Cell. 83:675-678.
    • (1995) Cell , vol.83 , pp. 675-678
    • Rootman, M.D.1    Berridge, M.J.2
  • 3
    • 0017301869 scopus 로고
    • Terbium emission as a probe of calcium binding sites in proteins
    • Brittain, H.G., F.S. Richardson, and R.B. Martin. 1976. Terbium emission as a probe of calcium binding sites in proteins. J. Am. Chem. Soc. 98:8255-8260.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 8255-8260
    • Brittain, H.G.1    Richardson, F.S.2    Martin, R.B.3
  • 4
    • 0030467311 scopus 로고    scopus 로고
    • The plasma-membrane calcium pump: Recent developments and future perspectives
    • Carafoli, E., E. Garciamartin, and D. Guerini. 1996. The plasma-membrane calcium pump: Recent developments and future perspectives. Experientia. 52:1091-1100.
    • (1996) Experientia , vol.52 , pp. 1091-1100
    • Carafoli, E.1    Garciamartin, E.2    Guerini, D.3
  • 5
    • 0021185585 scopus 로고
    • Activation of calmodulin by various meta cations as a function of ionic radius
    • Chao, S.H., Y. Suzuki, J.R. Zysk, and W.Y. Cheung. 1984. Activation of calmodulin by various meta cations as a function of ionic radius. Mol. Pharmacol. 26:75-82.
    • (1984) Mol. Pharmacol. , vol.26 , pp. 75-82
    • Chao, S.H.1    Suzuki, Y.2    Zysk, J.R.3    Cheung, W.Y.4
  • 9
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D.E. 1995. Calcium signaling. Cell. 80:259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 10
    • 0027463062 scopus 로고
    • Structure of a sarcoplasmic calcium-binding protein from amphioxus revined at 2.4 Å resolution
    • Cook, W.J., L.C. Jeffrey, and J.A. Cox. 1993. Structure of a sarcoplasmic calcium-binding protein from amphioxus revined at 2.4 Å resolution. J. Mol. Biol. 229:461-471.
    • (1993) J. Mol. Biol. , vol.229 , pp. 461-471
    • Cook, W.J.1    Jeffrey, L.C.2    Cox, J.A.3
  • 11
    • 0021039675 scopus 로고
    • Calcium binding proteins: Optical stopped-flow and proton NMR studies of the binding of lanthanide metal ions to parvalbumin
    • Corson, D.C., T.C. Williams, and B.D. Sykes. 1983. Calcium binding proteins: optical stopped-flow and proton NMR studies of the binding of lanthanide metal ions to parvalbumin. Biochemistry. 22:5882-5889.
    • (1983) Biochemistry , vol.22 , pp. 5882-5889
    • Corson, D.C.1    Williams, T.C.2    Sykes, B.D.3
  • 14
    • 0025870926 scopus 로고
    • Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments
    • Declercq, J.-P., B. Tinant, J. Parello, and J. Rambaud. 1991. Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments. J. Mol. Biol. 220:1017-1039.
    • (1991) J. Mol. Biol. , vol.220 , pp. 1017-1039
    • Declercq, J.-P.1    Tinant, B.2    Parello, J.3    Rambaud, J.4
  • 15
    • 0027340391 scopus 로고
    • 2+-binding activity in mutated EF-hands of cardiac troponin C
    • 2+-binding activity in mutated EF-hands of cardiac troponin C. J. Biol. Chem. 268:24067-24073.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24067-24073
    • Dotson, D.G.1    Putkey, J.A.2
  • 16
    • 0029670819 scopus 로고    scopus 로고
    • Kinetic tuning of the EF-hand calcium binding motif: The gateway residue independently adjusts (i) barrier height and (ii) equilibrium
    • Drake, S.K., and J.J. Falke. 1996. Kinetic tuning of the EF-hand calcium binding motif: the gateway residue independently adjusts (i) barrier height and (ii) equilibrium. Biochemistry. 35:1753-1760.
    • (1996) Biochemistry , vol.35 , pp. 1753-1760
    • Drake, S.K.1    Falke, J.J.2
  • 17
    • 0029954447 scopus 로고    scopus 로고
    • Tuning the equilibrium ion affinity and selectivity of the EF-hand calcium binding motif: Substitutions at the gateway position
    • Drake, S.K., K.L. Lee, and J.J. Falke. 1996. Tuning the equilibrium ion affinity and selectivity of the EF-hand calcium binding motif: substitutions at the gateway position. Biochemistry. 35:6697-6705.
    • (1996) Biochemistry , vol.35 , pp. 6697-6705
    • Drake, S.K.1    Lee, K.L.2    Falke, J.J.3
  • 18
    • 0030790043 scopus 로고    scopus 로고
    • Optimizing the metal binding parameters of an EF-hand-like calcium chelation loop: Coordinating side chains play a more important tuning role than chelation loop flexibility
    • In press
    • Drake, S.K., M.A. Zimmer, and J.J. Falke. 1997. Optimizing the metal binding parameters of an EF-hand-like calcium chelation loop: coordinating side chains play a more important tuning role than chelation loop flexibility. Biochemistry. In press.
    • (1997) Biochemistry
    • Drake, S.K.1    Zimmer, M.A.2    Falke, J.J.3
  • 19
    • 0027945446 scopus 로고
    • Molecular tuning of ion binding to calcium signaling proteins
    • Falke, J.J., S.K. Drake, A.L. Hazard, and O.B. Peersen. 1994. Molecular tuning of ion binding to calcium signaling proteins. Q. Rev. Biophys. 27:219-290.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 219-290
    • Falke, J.J.1    Drake, S.K.2    Hazard, A.L.3    Peersen, O.B.4
  • 20
    • 0025950774 scopus 로고
    • Quantitating and engineering the ion specificity of an EF-hand-like calcium binding site
    • Falke, J.J., E.E. Snyder, K.C. Thatcher, and C.S. Voertler. 1991. Quantitating and engineering the ion specificity of an EF-hand-like calcium binding site. Biochemistry. 30:8690-8697.
    • (1991) Biochemistry , vol.30 , pp. 8690-8697
    • Falke, J.J.1    Snyder, E.E.2    Thatcher, K.C.3    Voertler, C.S.4
  • 21
    • 0030936958 scopus 로고    scopus 로고
    • Mechanism of direct coupling between binding and calcium-induced structural change
    • Gagne, S.M., M.X. Li, and B.D. Sykes. 1997. Mechanism of direct coupling between binding and calcium-induced structural change. Biochemistry. 36:4386-4392.
    • (1997) Biochemistry , vol.36 , pp. 4386-4392
    • Gagne, S.M.1    Li, M.X.2    Sykes, B.D.3
  • 22
    • 0028987937 scopus 로고
    • Calcium signaling in neurons: Molecular mechanisms and cellular consequences
    • Ghosh, A., and M.E. Greenberg. 1995. Calcium signaling in neurons: molecular mechanisms and cellular consequences. Science (Wash. DC). 268:239-247.
    • (1995) Science (Wash. DC) , vol.268 , pp. 239-247
    • Ghosh, A.1    Greenberg, M.E.2
  • 24
    • 0022531495 scopus 로고
    • Calcium channel selectivity for divalent and monovalent cations
    • Hess, P., J.B. Lansman, and R.W. Tsien. 1986. Calcium channel selectivity for divalent and monovalent cations. J. Gen. Physiol. 88: 293-319.
    • (1986) J. Gen. Physiol. , vol.88 , pp. 293-319
    • Hess, P.1    Lansman, J.B.2    Tsien, R.W.3
  • 25
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science (Wash. DC). 268:1144-1149.
    • (1995) Science (Wash. DC) , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 26
    • 0027525244 scopus 로고
    • Luminescence spectroscopy
    • Horrocks, W.D. 1993. Luminescence spectroscopy. Methods Enzymol. 226:495-538.
    • (1993) Methods Enzymol. , vol.226 , pp. 495-538
    • Horrocks, W.D.1
  • 27
    • 0003224653 scopus 로고
    • Lanthanide ion luminescence in coordination chemistry and biochemistry
    • Horrocks, W.D., and M. Albin. 1984. Lanthanide ion luminescence in coordination chemistry and biochemistry. Prog. Inorg. Chem. 31:1-104.
    • (1984) Prog. Inorg. Chem. , vol.31 , pp. 1-104
    • Horrocks, W.D.1    Albin, M.2
  • 28
    • 0030032040 scopus 로고    scopus 로고
    • Calcium-binding and conformational response in EF-hand proteins
    • Ikura, M. 1996. Calcium-binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21:14-17.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 14-17
    • Ikura, M.1
  • 29
    • 0028678827 scopus 로고
    • Calcium binding proteins. 1. EF-hands
    • Kawasaki, H., and R.H. Kretsinger. 1994. Calcium binding proteins. 1. EF-hands. Protein Profiles. 1:343-517.
    • (1994) Protein Profiles , vol.1 , pp. 343-517
    • Kawasaki, H.1    Kretsinger, R.H.2
  • 31
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein
    • Kretsinger, R.H., and C.E. Nockolds. 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
  • 32
    • 0025191418 scopus 로고
    • Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5 Å resolution
    • Kumar, V.D., L. Lee, and B.F.P. Edwards. 1990. Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5 Å resolution. Biochemistry. 29:1404-1412.
    • (1990) Biochemistry , vol.29 , pp. 1404-1412
    • Kumar, V.D.1    Lee, L.2    Edwards, B.F.P.3
  • 33
    • 0029000375 scopus 로고
    • Quantitative measurements of the cooperativity in an EF-hand protein with sequential calcium binding
    • Linse, S., and W.J. Chazin. 1995. Quantitative measurements of the cooperativity in an EF-hand protein with sequential calcium binding. Prot. Sci. 4:1038-1044.
    • (1995) Prot. Sci. , vol.4 , pp. 1038-1044
    • Linse, S.1    Chazin, W.J.2
  • 37
    • 0003930168 scopus 로고
    • John Wiles, and Sons Limited, Chichester, UK
    • Marcus, Y. 1985. Ion Solvation. John Wiles, and Sons Limited, Chichester, UK. pp. 164.
    • (1985) Ion Solvation , pp. 164
    • Marcus, Y.1
  • 38
    • 0025367420 scopus 로고
    • Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments
    • Marsden, B.J., G.S. Shaw, and B.D. Sykes. 1990. Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments. Biochem. Cell Biol. 68:587-601.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 587-601
    • Marsden, B.J.1    Shaw, G.S.2    Sykes, B.D.3
  • 40
    • 0016434266 scopus 로고
    • Terbium replacement of calcium in carp muscle parvalbumin: An X-ray crystallographic study
    • Moews, P.C., and R.H. Kretsinger. 1975. Terbium replacement of calcium in carp muscle parvalbumin: an X-ray crystallographic study. J. Mol. Biol. 91:229-232.
    • (1975) J. Mol. Biol. , vol.91 , pp. 229-232
    • Moews, P.C.1    Kretsinger, R.H.2
  • 43
    • 0025033871 scopus 로고
    • Site-specific replacement of amino acid residues within the CD binding loop of rat oncomodulin
    • Palmisano, W.A., C.L. Treviño, and M.T. Henzl. 1990. Site-specific replacement of amino acid residues within the CD binding loop of rat oncomodulin. J. Biol. Chem. 265:14450-14456.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14450-14456
    • Palmisano, W.A.1    Treviño, C.L.2    Henzl, M.T.3
  • 44
    • 0028799234 scopus 로고
    • Divalent cation selectivity in a cyclic nucleotide-gated ion channel
    • Park, C.-S., and R. MacKinnon. 1995. Divalent cation selectivity in a cyclic nucleotide-gated ion channel. Biochemistry. 34:13328-13333.
    • (1995) Biochemistry , vol.34 , pp. 13328-13333
    • Park, C.-S.1    MacKinnon, R.2
  • 45
    • 0028097832 scopus 로고
    • A structure-activity study of calcium affinity and selectivity using a synthetic peptide model of the helix-loop-helix calcium-binding motif
    • Procyshyn, R.M., and R.E. Reid. 1994. A structure-activity study of calcium affinity and selectivity using a synthetic peptide model of the helix-loop-helix calcium-binding motif. J. Biol. Chem. 269: 1641-1647.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1641-1647
    • Procyshyn, R.M.1    Reid, R.E.2
  • 46
    • 0019887829 scopus 로고
    • Calcium-induced protein folding. Structure-affinity relationships in synthetic analogs of the helix-loop-helix calcium binding unit
    • Reid, R.E., J. Gariépy, A.K. Saund, and R.S. Hodges. 1981. Calcium-induced protein folding. Structure-affinity relationships in synthetic analogs of the helix-loop-helix calcium binding unit. J. Biol. Chem. 256:2742-2751.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2742-2751
    • Reid, R.E.1    Gariépy, J.2    Saund, A.K.3    Hodges, R.S.4
  • 49
    • 84944648082 scopus 로고
    • Revised effective ionic radii
    • Shannon, R.D. 1976. Revised effective ionic radii. Acta Crystallogr. A32:751-767.
    • (1976) Acta Crystallogr. , vol.A32 , pp. 751-767
    • Shannon, R.D.1
  • 51
    • 0025355493 scopus 로고
    • Calcium-site specificity: Effect of size and charge on metal ion binding to an EF-hand-like site
    • Snyder, E.E., B.W. Buoscio, and J.J. Falke. 1990. Calcium-site specificity: effect of size and charge on metal ion binding to an EF-hand-like site. Biochemistry. 29:3937-3943.
    • (1990) Biochemistry , vol.29 , pp. 3937-3943
    • Snyder, E.E.1    Buoscio, B.W.2    Falke, J.J.3
  • 53
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka, N.C.J., and M.N.G. James. 1989. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58:951-998.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-998
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 56
    • 0023256886 scopus 로고
    • A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
    • Vyas, N.K., M.N. Vyas, and F.A. Quiocho. 1987. A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis. Nature (Lond.). 327:635-638.
    • (1987) Nature (Lond.) , vol.327 , pp. 635-638
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 59
    • 0021491347 scopus 로고
    • Calcium binding proteins: Calcium-lanthanide exchange in carp parvalbumin
    • Williams, T.C., D.C. Corson, and B.D. Sykes. 1984. Calcium binding proteins: calcium-lanthanide exchange in carp parvalbumin. J. Am. Chem. Soc. 106:5698-5702.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5698-5702
    • Williams, T.C.1    Corson, D.C.2    Sykes, B.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.