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Volumn 5, Issue 7, 1996, Pages 1215-1228

Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences

Author keywords

calcium; calmodulin; CD; domains; mechanism; myosin light chain kinase; peptides; stopped flow

Indexed keywords

CALCIUM; CALMODULIN; EGTAZIC ACID; MYOSIN LIGHT CHAIN KINASE; SYNTHETIC PEPTIDE;

EID: 0030008340     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050701     Document Type: Article
Times cited : (143)

References (43)
  • 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
  • 3
    • 0027975838 scopus 로고
    • Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 Å resolution
    • Ban C, Ramakrishnan B, Ling KY, Kung C, Sundaralingam M. 1994. Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 Å resolution. Acta Crystallogr D 50:50-63.
    • (1994) Acta Crystallogr D , vol.50 , pp. 50-63
    • Ban, C.1    Ramakrishnan, B.2    Ling, K.Y.3    Kung, C.4    Sundaralingam, M.5
  • 4
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici A, Ikura M. 1995. Molecular and structural basis of target recognition by calmodulin. Annu Rev Biophys Biomol Struct 24:85-116.
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 5
    • 0028784853 scopus 로고
    • Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin
    • Findlay WA, Gradwell MJ, Bayley PM. 1995a. Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin. Protein Sci 4:2375-2382.
    • (1995) Protein Sci , vol.4 , pp. 2375-2382
    • Findlay, W.A.1    Gradwell, M.J.2    Bayley, P.M.3
  • 6
    • 0028965961 scopus 로고
    • Recovery of native structure by calcium binding site mutants of calmodulin upon binding of sk-MLCK target peptides
    • Findlay WA, Martin SR, Beckingham K, Bayley PM. 1995b. Recovery of native structure by calcium binding site mutants of calmodulin upon binding of sk-MLCK target peptides. Biochemistry 34:2087-2094.
    • (1995) Biochemistry , vol.34 , pp. 2087-2094
    • Findlay, W.A.1    Martin, S.R.2    Beckingham, K.3    Bayley, P.M.4
  • 9
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 10
    • 0027278233 scopus 로고
    • Fluorescence anisotropy imaging microscopy maps calmodulin binding during cellular contraction and locomotion
    • Gough AH, Taylor DL. 1993. Fluorescence anisotropy imaging microscopy maps calmodulin binding during cellular contraction and locomotion. J Cell Biol 121:1095-1107.
    • (1993) J Cell Biol , vol.121 , pp. 1095-1107
    • Gough, A.H.1    Taylor, D.L.2
  • 12
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. 1992. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256:632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 13
    • 0025866660 scopus 로고
    • Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light chain kinase: Indication of a conformational change in the central helix
    • Ikura M, Kay LE, Krinks M, Bax A. 1991. Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light chain kinase: indication of a conformational change in the central helix. Biochemistry 30:5498-5504.
    • (1991) Biochemistry , vol.30 , pp. 5498-5504
    • Ikura, M.1    Kay, L.E.2    Krinks, M.3    Bax, A.4
  • 15
    • 0017355688 scopus 로고
    • 2+ to the protein activator of 3′,5′-cyclic adenosine mono-phosphate phosphodiesterase
    • 2+ to the protein activator of 3′,5′-cyclic adenosine mono-phosphate phosphodiesterase. Biochemistry 16:1017-1024.
    • (1977) Biochemistry , vol.16 , pp. 1017-1024
    • Klee, C.B.1
  • 19
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • Linse S, Helmersson A, Forsén S. 1991a. 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    Forsén, S.3
  • 21
    • 0028982260 scopus 로고
    • 2+-regulated dynamic compartmentalization of calmodulin in living smooth muscle cells
    • 2+-regulated dynamic compartmentalization of calmodulin in living smooth muscle cells. J Biol Chem 270:21532-21538.
    • (1995) J Biol Chem , vol.270 , pp. 21532-21538
    • Luby-Phelps, K.1    Hori, M.2    Phelps, J.M.3    Won, D.4
  • 22
    • 0026530375 scopus 로고
    • Stopped-flow studies of calcium dissociation from calcium-binding-site mutants of Drosophila melanogaster calmodulin
    • Martin SR, Maune JF, Beckingham K, Bayley PM. 1992. Stopped-flow studies of calcium dissociation from calcium-binding-site mutants of Drosophila melanogaster calmodulin. 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
  • 23
    • 0029990420 scopus 로고    scopus 로고
    • Spectroscopic characterization of a high affinity calmodulin-target peptide hybrid molecule
    • Martin SR, Bayley PM, Brown SE, Porumb T, Zhang M, Ikura M. 1996. Spectroscopic characterization of a high affinity calmodulin-target peptide hybrid molecule. Biochemistry 35:3508-3517.
    • (1996) Biochemistry , vol.35 , pp. 3508-3517
    • Martin, S.R.1    Bayley, P.M.2    Brown, S.E.3    Porumb, T.4    Zhang, M.5    Ikura, M.6
  • 24
    • 0021078714 scopus 로고
    • Structural changes in melittin and calmodulin upon complex formation and their modulation by calcium
    • Maulet Y, Cox JA. 1983. Structural changes in melittin and calmodulin upon complex formation and their modulation by calcium. Biochemistry 22: 5680-5686.
    • (1983) Biochemistry , vol.22 , pp. 5680-5686
    • Maulet, Y.1    Cox, J.A.2
  • 26
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • Meador WE, Means AR, Quiocho FA. 1992. Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257:1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 27
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador WE, Means AR, Quiocho FA. 1993. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262:1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 29
    • 0022318905 scopus 로고
    • Calcium binding to complexes of calmodulin and calmodulin binding proteins
    • Olwin BR, Storm DT. 1985. Calcium binding to complexes of calmodulin and calmodulin binding proteins. Biochemistry 24:8081-8086.
    • (1985) Biochemistry , vol.24 , pp. 8081-8086
    • Olwin, B.R.1    Storm, D.T.2
  • 30
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices
    • O'Neil KT, DeGrado WF. 1990. How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices. Trends Biochem Sci 15:59-64.
    • (1990) Trends Biochem Sci , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 31
    • 0028305218 scopus 로고
    • Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments
    • Persechini A, McMillan K, Leakey P. 1994. Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments. J Biol Chem 269:16148-16154.
    • (1994) J Biol Chem , vol.269 , pp. 16148-16154
    • Persechini, A.1    McMillan, K.2    Leakey, P.3
  • 32
    • 0029671422 scopus 로고    scopus 로고
    • 2+ dissociation from complexes of calmodulin with nitric oxide synthase or myosin light chain kinase
    • 2+ dissociation from complexes of calmodulin with nitric oxide synthase or myosin light chain kinase. J Biol Chem 271:62-67.
    • (1996) J Biol Chem , vol.271 , pp. 62-67
    • Persechini, A.1    White, H.D.2    Gansz, K.J.3
  • 33
    • 0028037632 scopus 로고
    • Determination of calcium binding constants by flow dialysis
    • Porumb T. 1994. Determination of calcium binding constants by flow dialysis. Anal Biochem 220:227-237.
    • (1994) Anal Biochem , vol.220 , pp. 227-237
    • Porumb, T.1
  • 35
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying lengths in water
    • Scholtz JM, Qian H, York EJ, Stewart JM, Baldwin RL. 1991. Parameters of helix-coil transition theory for alanine-based peptides of varying lengths in water. Biopolymers 31:1463-1470.
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 36
    • 0027415728 scopus 로고
    • A model for the calmodulin-peptide complex based on the troponin C crystal packing and its similarity to the NMR structure of the calmodulin-myosin light chain kinase peptide complex
    • Sekharudu CY, Sundaralingam M. 1993. A model for the calmodulin-peptide complex based on the troponin C crystal packing and its similarity to the NMR structure of the calmodulin-myosin light chain kinase peptide complex. Protein Sci 2:620-625.
    • (1993) Protein Sci , vol.2 , pp. 620-625
    • Sekharudu, C.Y.1    Sundaralingam, M.2
  • 37
    • 0025372502 scopus 로고
    • Model for the interaction of amphiphilic helices with troponin C and calmodulin
    • Strynadka NCJ, James MNG. 1990. Model for the interaction of amphiphilic helices with troponin C and calmodulin. Proteins Struct Funct Genet 7:234-248.
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 234-248
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 38
    • 0025719432 scopus 로고
    • Structure of recombinant calmodulin from Drosophila melanogaster refined at 2.2 Å resolution
    • Taylor DA, Sack JS, Maune JF, Beckingham K, Quiocho FA. 1991. Structure of 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
  • 39
    • 0029058666 scopus 로고
    • Structural analysis of a novel interaction by calmodulin: High-affinity binding of a peptide in the absence of calcium
    • Urbauer JL, Short JH, Dow LK, Wand AJ. 1995. Structural analysis of a novel interaction by calmodulin: High-affinity binding of a peptide in the absence of calcium. Biochemistry 34:8099-8109.
    • (1995) Biochemistry , vol.34 , pp. 8099-8109
    • Urbauer, J.L.1    Short, J.H.2    Dow, L.K.3    Wand, A.J.4
  • 42
    • 0026658959 scopus 로고
    • Binding of calcium by calmodulin: Influence of the calmodulin binding domain of the plasma membrane calcium pump
    • Yazawa M, Vorherr T, James P, Carafoli E, Yagi K. 1992. Binding of calcium by calmodulin: Influence of the calmodulin binding domain of the plasma membrane calcium pump. Biochemistry 31:3171-3176.
    • (1992) Biochemistry , vol.31 , pp. 3171-3176
    • Yazawa, M.1    Vorherr, T.2    James, P.3    Carafoli, E.4    Yagi, K.5
  • 43
    • 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


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