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Volumn 3, Issue 9, 1996, Pages 788-795

C2 domain conformational changes in phospholipase C-δ1

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM DERIVATIVE; PHOSPHATIDYLINOSITIDE; PHOSPHOLIPASE C;

EID: 0029772577     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0996-788     Document Type: Article
Times cited : (102)

References (45)
  • 1
    • 0026654469 scopus 로고
    • Regulation of inositol phospholipid-specific phospholipase C isozymes
    • Rhee, S.G. & Choi, K.D. Regulation of inositol phospholipid-specific phospholipase C isozymes. J. Biol. Chem. 267, 12393-12396 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 12393-12396
    • Rhee, S.G.1    Choi, K.D.2
  • 2
    • 0028986998 scopus 로고
    • 2 hydrolysis and regulation of phospholipase C isozymes
    • 2 hydrolysis and regulation of phospholipase C isozymes. Curr. Opinion Cell Biol. 7, 183-189 (1995).
    • (1995) Curr. Opinion Cell Biol. , vol.7 , pp. 183-189
    • Lee, S.B.1    Rhee, S.G.2
  • 4
    • 0028787055 scopus 로고
    • 1, binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
    • 1, binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes. Biochemistry 34, 16228-16234 (1995).
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1
  • 5
    • 0029416974 scopus 로고
    • 1, requires a pleckstrin homology domain for interaction with the plasma membrane
    • 1, requires a pleckstrin homology domain for interaction with the plasma membrane. Biochem. J. 312, 661-666 (1995).
    • (1995) Biochem. J. , vol.312 , pp. 661-666
    • Paterson, H.F.1
  • 6
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen, L-O., Perisic, O., Cheung, R., Katan, M. & Williams, R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380, 595-602 (1996).
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.-O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 8
    • 0029364428 scopus 로고
    • Seeing two domains
    • Newton, A.C. Seeing two domains. Current Biol. 5, 973-976 (1995).
    • (1995) Current Biol. , vol.5 , pp. 973-976
    • Newton, A.C.1
  • 9
    • 0030034251 scopus 로고    scopus 로고
    • Extending the C2 domain family: C2s in PKCs δ, ε, η, θ, phospholipases, GAPs, and perforin
    • Ponting, C.P. & Parker, P. Extending the C2 domain family: C2s in PKCs δ, ε, η, θ, phospholipases, GAPs, and perforin. Prot. Sci. 5, 162-166 (1996).
    • (1996) Prot. Sci. , vol.5 , pp. 162-166
    • Ponting, C.P.1    Parker, P.2
  • 10
    • 0028337397 scopus 로고
    • Structure of the regulatory domains of the src-family tyrosine kinase lck
    • Eck, M.J., Atwell, S.K., Shoelson, S.E. & Harrison, S.C. Structure of the regulatory domains of the src-family tyrosine kinase lck. Nature 268, 764-769 (1994).
    • (1994) Nature , vol.268 , pp. 764-769
    • Eck, M.J.1    Atwell, S.K.2    Shoelson, S.E.3    Harrison, S.C.4
  • 11
    • 0028938153 scopus 로고
    • Crystal structure of the mammalian Grb2 adaptor
    • Maignan, S. et al. Crystal structure of the mammalian Grb2 adaptor. Science 268, 291-293 (1995).
    • (1995) Science , vol.268 , pp. 291-293
    • Maignan, S.1
  • 12
    • 84988043558 scopus 로고
    • Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor
    • Hatada, M. et al. Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. Nature 377, 32-38 (1995).
    • (1995) Nature , vol.377 , pp. 32-38
    • Hatada, M.1
  • 13
    • 0030066325 scopus 로고    scopus 로고
    • Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2
    • Eck, M.J, Pluskey, S., Trub, T, Harrison. S.C. & Shoelson, S.E. Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature 379, 277-280 (1996).
    • (1996) Nature , vol.379 , pp. 277-280
    • Eck, M.J.1    Pluskey, S.2    Trub, T.3    Harrison, S.C.4    Shoelson, S.E.5
  • 14
    • 0025734618 scopus 로고
    • Properties of phospholipase C isozymes
    • Takenawa, T., Homma, Y. & Emori, Y. Properties of phospholipase C isozymes. Methods Enzymol. 197, 511-517 (1991).
    • (1991) Methods Enzymol. , vol.197 , pp. 511-517
    • Takenawa, T.1    Homma, Y.2    Emori, Y.3
  • 16
    • 0027461517 scopus 로고
    • Structural requirements of phosphatidylinositol-specific phospholipase C5, for enzyme activity
    • Ellis, M.V., Carne, A. & Katan, M. Structural requirements of phosphatidylinositol-specific phospholipase C5, for enzyme activity. Eur. J. Biochem. 213, 339-347 (1993).
    • (1993) Eur. J. Biochem. , vol.213 , pp. 339-347
    • Ellis, M.V.1    Carne, A.2    Katan, M.3
  • 18
    • 0028068586 scopus 로고
    • 2+-dependent interaction of the cytoplasmic region of synaptotagmin with membranes
    • 2+-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. J. Biol. Chem. 269, 5735-5741 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 5735-5741
    • Chapman, E.R.1    Jahn, R.2
  • 19
    • 0025810578 scopus 로고
    • 2+-dependent translocation domain with homology to PKC and GAP
    • 2+-dependent translocation domain with homology to PKC and GAP. Cell. 65, 1043-1051 (1991).
    • (1991) Cell , vol.65 , pp. 1043-1051
    • Clark, J.D.1
  • 20
    • 0028339812 scopus 로고
    • 2+-independent catalytic domain
    • 2+-independent catalytic domain. J. Biol. Chem. 269, 18239-18249 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18239-18249
    • Nafelski, E.A.1
  • 21
    • 0016378745 scopus 로고
    • Binding of lanthanide ions to thermolysin
    • Matthews, B.W. & Weaver, L.H. Binding of lanthanide ions to thermolysin. Biochemisrty 13, 1719-1725 (1974).
    • (1974) Biochemisrty , vol.13 , pp. 1719-1725
    • Matthews, B.W.1    Weaver, L.H.2
  • 25
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T. & Ikura, M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct. Biol. 2, 758-767 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 26
    • 0029159794 scopus 로고
    • Solution structure of calcium-free calmodulin
    • Kuboniwa, H. et al. Solution structure of calcium-free calmodulin. Nature Struct. Biol. 2, 768-776 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 768-776
    • Kuboniwa, H.1
  • 27
    • 0025047629 scopus 로고
    • A mutant T4 lysozyme displays five different crystal conformations
    • Faber, H.R. & Matthews, B.W. A mutant T4 lysozyme displays five different crystal conformations. Nature 34B, 263-266 (1990).
    • (1990) Nature , vol.34 B , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 28
    • 0028172171 scopus 로고
    • 2+-dependent conformational change in synaptotagmin I
    • 2+-dependent conformational change in synaptotagmin I. J. Biol. Chem. 269, 28547-28550 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 28547-28550
    • Davletov, B.A.1    Sudhof, T.C.2
  • 30
    • 0025170867 scopus 로고
    • Protein kinase C interaction with calcium: A phospholipid-dependent process
    • Bazzi, M.D. & Nelsestuen, G.L Protein kinase C interaction with calcium: a phospholipid-dependent process. Biochemistry 29, 7624-7630 (1990).
    • (1990) Biochemistry , vol.29 , pp. 7624-7630
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 31
    • 0026682675 scopus 로고
    • Interaction of protein kinase C with phosphatidylserine. 1. Cooperativity in lipid binding
    • Orr, J.W. & Newton, A.C. Interaction of protein kinase C with phosphatidylserine. 1. Cooperativity in lipid binding. Biochemistry 31, 4667-4673 (1992).
    • (1992) Biochemistry , vol.31 , pp. 4667-4673
    • Orr, J.W.1    Newton, A.C.2
  • 32
    • 0028341564 scopus 로고
    • Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containcng membranes
    • Newton, A.C. and Keranen, L.M. Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containcng membranes. Biochemistry 33, 6651-6658 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6651-6658
    • Newton, A.C.1    Keranen, L.M.2
  • 33
    • 0027470669 scopus 로고
    • Mechanism of activation of protein kinase C: Roles of diolein and phosphatidylserine
    • Mosior, M. & Epand, R.M. Mechanism of activation of protein kinase C: roles of diolein and phosphatidylserine. Biochemistry 32, 66-75 (1993).
    • (1993) Biochemistry , vol.32 , pp. 66-75
    • Mosior, M.1    Epand, R.M.2
  • 34
    • 0029872616 scopus 로고    scopus 로고
    • 2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV
    • 2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV. J. Biol. Chem. 271, 8430-8434 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8430-8434
    • Fukuda, M.1    Kojima, T.2    Mikoshiba, K.3
  • 36
    • 84920325457 scopus 로고
    • AMoRE- An automated package for molecular replacement
    • Navaza, J. AMoRE- an automated package for molecular replacement. Acta Crystallogr. A50, 157-163 (1994).
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 38
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, No. 4. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 39
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42, 140-149 (1986).
    • (1986) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Read, R.J.1
  • 40
    • 84913050729 scopus 로고
    • An efficient general-purpose least squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F. & Matthews, B.W. An efficient general-purpose least squares refinement program for macromolecular structures. Acta Crystallogr. A43, 489-501 (1987).
    • (1987) Acta Crystallogr. , vol.A43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 41
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh, R.A. & Huber, R. Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallogr. A47, 392-400 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjelgard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgard, M.4
  • 44
    • 0026244229 scopus 로고
    • MOLSCRIPT- A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. MOLSCRIPT- a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 45
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M. Ribbon models of macromolecules. J. Mol. Graphics 5, 103-106 (1987).
    • (1987) J. Mol. Graphics , vol.5 , pp. 103-106
    • Carson, M.1


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