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Volumn 280, Issue 3, 1998, Pages 485-500

Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2

Author keywords

C2 domain; Calcium dependent lipid binding; Cytosolic phospholipase A2; NMR structure; Phosphocholine

Indexed keywords

CALCIUM ION; PHOSPHOLIPASE A2;

EID: 0032540860     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1874     Document Type: Article
Times cited : (101)

References (44)
  • 1
    • 0028988377 scopus 로고
    • 15N assignments and secondary structure of the GTPase activating of Gs
    • 15N assignments and secondary structure of the GTPase activating of Gs. Biochemistry. 34:1995;155-162
    • (1995) Biochemistry , vol.34 , pp. 155-162
    • Benjamin, D.1    Markby, D.2    Bourne, H.3    Kuntz, I.4
  • 6
    • 0025230269 scopus 로고
    • Calcium- and magnesium-binding properties of oncomodulin: Direct binding studies and microcalorimetry
    • Cox J.A., Milos M., MacManus J.P. Calcium- and magnesium-binding properties of oncomodulin Direct binding studies and microcalorimetry. J. Biol. Chem. 265:1990;6633-6637
    • (1990) J. Biol. Chem. , vol.265 , pp. 6633-6637
    • Cox, J.A.1    Milos, M.2    MacManus, J.P.3
  • 8
    • 0028172171 scopus 로고
    • 2+-dependent Conformational change in synaptotagmin I
    • 2+-dependent Conformational change in synaptotagmin I. J. Biol. Chem. 269:1994;28547-28550
    • (1994) J. Biol. Chem. , vol.269 , pp. 28547-28550
    • Daveletov, B.A.1    Südhof, T.C.2
  • 9
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen L.O., Perisic O., Cheung R., Katan M., Williams R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature. 380:1996;595-602
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 10
    • 0030933176 scopus 로고    scopus 로고
    • A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-delta1
    • Essen L.O., Perisic O., Lynch D.E., Katan M., Williams R.L. A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-delta1. Biochemistry. 36:1997;2753-2762
    • (1997) Biochemistry , vol.36 , pp. 2753-2762
    • Essen, L.O.1    Perisic, O.2    Lynch, D.E.3    Katan, M.4    Williams, R.L.5
  • 12
    • 0030967642 scopus 로고    scopus 로고
    • Similarity between C2 domain jaws and immunoglobulin CDRs
    • Grobler J., Hurley J. Similarity between C2 domain jaws and immunoglobulin CDRs. Nature Struct. Biol. 4:1997;261-262
    • (1997) Nature Struct. Biol. , vol.4 , pp. 261-262
    • Grobler, J.1    Hurley, J.2
  • 14
    • 0028672795 scopus 로고
    • Methods to study membrane protein structure in solution
    • Henry G.D., Sykes B.D. Methods to study membrane protein structure in solution. Methods Enzymol. 239:1994;515-535
    • (1994) Methods Enzymol. , vol.239 , pp. 515-535
    • Henry, G.D.1    Sykes, B.D.2
  • 16
    • 0030755311 scopus 로고    scopus 로고
    • Protein kinase C and phospholipase C: Bilayer interactions and regulation
    • Hurley J.H., Grobler J.A. Protein kinase C and phospholipase C bilayer interactions and regulation. Curr. Opin. Struct. Biol. 7:1997;557-565
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 557-565
    • Hurley, J.H.1    Grobler, J.A.2
  • 17
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL a program for display and analysis of macromolecular structures. J. Mol. Graphics. 14:1996;51-55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 18
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski R., Rullmannn J., MacArthur M., Kaptein R., Thorton J.M. AQUA and PROCHECK-NMR programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.1    Rullmannn, J.2    MacArthur, M.3    Kaptein, R.4    Thorton, J.M.5
  • 21
    • 0023006138 scopus 로고
    • Calcium-proton and calcium-magnesium antagonisms in calmodulin: Microcalorimetric and potentiometric analyses
    • Milos M., Schaer J.J., Comte M., Cox J.A. Calcium-proton and calcium-magnesium antagonisms in calmodulin microcalorimetric and potentiometric analyses. Biochemistry. 25:1986;6279-6287
    • (1986) Biochemistry , vol.25 , pp. 6279-6287
    • Milos, M.1    Schaer, J.J.2    Comte, M.3    Cox, J.A.4
  • 22
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram D.R., Kay L.E. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. Ser. B. 103:1994;203-216
    • (1994) J. Magn. Reson. Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 23
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski E.A., Falke J.J. The C2 domain calcium-binding motif structural and functional diversity. Protein Sci. 5:1996;2375-2390
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 25
    • 0030612437 scopus 로고    scopus 로고
    • 2+-signalling cycle of a membrane-docking C2 domain
    • 2+-signalling cycle of a membrane-docking C2 domain. Biochemistry. 36:1997;12011-12018
    • (1997) Biochemistry , vol.36 , pp. 12011-12018
    • Nalefski, E.A.1    Slazas, M.2    Falke, J.3
  • 27
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton A.C. Protein kinase C structure, function, and regulation. J. Biol. Chem. 270:1995;28495-28498
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 29
    • 0030034251 scopus 로고    scopus 로고
    • Extending the C2 domain family: C2s in PKCs delta, epsilon, eta, theta, phospholipases, GAPs, and perforin
    • Ponting C., Parker P. Extending the C2 domain family C2s in PKCs delta, epsilon, eta, theta, phospholipases, GAPs, and perforin. Protein Sci. 5:1996;162-166
    • (1996) Protein Sci. , vol.5 , pp. 162-166
    • Ponting, C.1    Parker, P.2
  • 30
    • 0027200551 scopus 로고
    • Sub-cellular localization of prostaglandin endoperoxide synthase 2 in murine 3T3 cells
    • Regier M., DeWitt D., Schindler M., Smith W. Sub-cellular localization of prostaglandin endoperoxide synthase 2 in murine 3T3 cells. Arch. Biochem. Biophys. 301:1993;439-444
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 439-444
    • Regier, M.1    Dewitt, D.2    Schindler, M.3    Smith, W.4
  • 31
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 a
    • Satow Y., Cohen G., Padlan E., Davies D. Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A. J. Mol. Biol. 190:1986;593-604
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.2    Padlan, E.3    Davies, D.4
  • 35
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof T.C. The synaptic vesicle cycle a cascade of protein-protein interactions. Nature. 375:1995;645-653
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 36
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman J., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica a prototypic acetylcholine-binding protein. Science. 253:1991;872-879
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 38
  • 40
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J., Lin L. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:1989;131-137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.3    Lin, L.4
  • 41
    • 0027504207 scopus 로고
    • 5-lipoxygenase and 5-lipoxygenase-activating protein are localized in the nuclear envelope of activated human leukocytes
    • Woods J., Evans J., Ethier D., Scott S., Vickers P., Hearn L., Heibein J., Charleson S., Singer I. 5-lipoxygenase and 5-lipoxygenase-activating protein are localized in the nuclear envelope of activated human leukocytes. J. Exp. Med. 178:1993;1935-1946
    • (1993) J. Exp. Med. , vol.178 , pp. 1935-1946
    • Woods, J.1    Evans, J.2    Ethier, D.3    Scott, S.4    Vickers, P.5    Hearn, L.6    Heibein, J.7    Charleson, S.8    Singer, I.9
  • 42
    • 0030239095 scopus 로고    scopus 로고
    • Complete 1H, 15N and 13C assignments, secondary structure, and topology of recombinant human interleukin-6
    • Xu G.Y., Hong J., McDonagh T., Stahl M., Kay L.E., Seehra J., Cumming D.A. Complete 1H, 15N and 13C assignments, secondary structure, and topology of recombinant human interleukin-6. J. Biomol. NMR. 8:1996;123-135
    • (1996) J. Biomol. NMR , vol.8 , pp. 123-135
    • Xu, G.Y.1    Hong, J.2    McDonagh, T.3    Stahl, M.4    Kay, L.E.5    Seehra, J.6    Cumming, D.A.7
  • 44
    • 0031064317 scopus 로고    scopus 로고
    • Triple-resonance NOESY-based experiments with improved spectral resolution: Application to structural characterization of unfolded, partially folded and folded proteins
    • Zhang O., Forman-Kay J.D., Shortle D., Kay L.E. Triple-resonance NOESY-based experiments with improved spectral resolution application to structural characterization of unfolded, partially folded and folded proteins. J. Biomol. NMR. 9:1997;181-200
    • (1997) J. Biomol. NMR , vol.9 , pp. 181-200
    • Zhang, O.1    Forman-Kay, J.D.2    Shortle, D.3    Kay, L.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.