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Volumn 279, Issue 1, 1998, Pages 223-232

Structures of two novel crystal forms of Naja naja naja phospholipase A2 lacking Ca2+ reveal trimeric packing

Author keywords

Arachidonate; Crystal; Lipase; Structure; Trimer

Indexed keywords

CALCIUM ION; PHOSPHOLIPASE A2;

EID: 0032577372     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1759     Document Type: Article
Times cited : (59)

References (47)
  • 5
    • 0029130345 scopus 로고
    • Lipid signaling enzymes and surface dilution kinetics
    • Carman G.M., Deems R.A., Dennis E.A. Lipid signaling enzymes and surface dilution kinetics. J. Biol. Chem. 270:1995;18711-18714
    • (1995) J. Biol. Chem , vol.270 , pp. 18711-18714
    • Carman, G.M.1    Deems, R.A.2    Dennis, E.A.3
  • 7
    • 0025091499 scopus 로고
    • 2 from snake venom to human secreted forms
    • 2 from snake venom to human secreted forms. J. Mol. Evol. 31:1990;228-238
    • (1990) J. Mol. Evol , vol.31 , pp. 228-238
    • Davidson, F.F.1    Dennis, E.A.2
  • 8
    • 0016710578 scopus 로고
    • 2 from cobra venom (Naja naja naja) that has a molecular weight of 11,000
    • 2 from cobra venom (Naja naja naja) that has a molecular weight of 11,000. J. Biol. Chem. 250:1975;9008-9012
    • (1975) J. Biol. Chem , vol.250 , pp. 9008-9012
    • Deems, R.A.1    Dennis, E.A.2
  • 9
    • 77956908706 scopus 로고
    • third edit. Boyer P.D. New York: Academic Press Ltd
    • Dennis E.A. third edit. Boyer P.D. The Enzymes. vol. 16:1983;307-353 Academic Press Ltd, New York
    • (1983) The Enzymes , vol.16 , pp. 307-353
    • Dennis, E.A.1
  • 10
    • 0023611323 scopus 로고
    • The regulation of eicosanoid production: Role of phospholipases and inhibitors
    • Dennis E.A. The regulation of eicosanoid production role of phospholipases and inhibitors. Bio/Technol. 5:1987;1294-1300
    • (1987) Bio/Technol , vol.5 , pp. 1294-1300
    • Dennis, E.A.1
  • 12
    • 0030614354 scopus 로고    scopus 로고
    • 2 superfamily of signal transduction enzymes
    • 2 superfamily of signal transduction enzymes. Trends Biochem. Sci. 22:1997;1-2
    • (1997) Trends Biochem. Sci , vol.22 , pp. 1-2
    • Dennis, E.A.1
  • 14
    • 0021105553 scopus 로고
    • 2 according to sequence. Evolutionary and pharmacological implications
    • 2 according to sequence. Evolutionary and pharmacological implications. Eur. J. Biochem. 137:1983;545-551
    • (1983) Eur. J. Biochem , vol.137 , pp. 545-551
    • Dufton, M.J.1    Hider, R.C.2
  • 16
    • 0022293584 scopus 로고
    • Multiwire area X-ray diffractometers
    • Hamlin R. Multiwire area X-ray diffractometers. Methods Enzymol. 114:1985;416-452
    • (1985) Methods Enzymol , vol.114 , pp. 416-452
    • Hamlin, R.1
  • 19
    • 0022326269 scopus 로고
    • Software for a diffractometer with multiwire area detector
    • Howard A.J., Nielsen C., Xuong N.H. Software for a diffractometer with multiwire area detector. Methods Enzymol. 114:1985;452-472
    • (1985) Methods Enzymol , vol.114 , pp. 452-472
    • Howard, A.J.1    Nielsen, C.2    Xuong, N.H.3
  • 20
    • 0001797984 scopus 로고
    • FRODO: A graphics fitting program for macromolecules
    • D. Sayre. Oxford: Clarendon Press
    • Jones T.A. FRODO a graphics fitting program for macromolecules. Sayre D. Computational Chemistry. 1982;303-317 Clarendon Press, Oxford
    • (1982) Computational Chemistry , pp. 303-317
    • Jones, T.A.1
  • 21
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallog sect. A. 47:1991;110-119
    • (1991) Acta Crystallog Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 24
    • 0001099937 scopus 로고
    • Traitment statistique des erreurs dans la determination des structures cristallines
    • Luzzati V. Traitment statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;805-810
    • (1952) Acta Crystallog , vol.5 , pp. 805-810
    • Luzzati, V.1
  • 25
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497
    • (1968) J. Mol. Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 32
    • 0022182544 scopus 로고
    • 2 and comparison with other phospholipases
    • 2 and comparison with other phospholipases. J. Biol. Chem. 260:1985;11099-11106
    • (1985) J. Biol. Chem , vol.260 , pp. 11099-11106
    • Pluckthun, A.1    Dennis, E.A.2
  • 43
    • 9844252960 scopus 로고
    • San Francisco: School of Pharmacy University of California at San Francisco
    • UCSF MidasPlus User's Manual. 1995;School of Pharmacy University of California at San Francisco, San Francisco
    • (1995) UCSF MidasPlus User's Manual
  • 46
    • 0028787430 scopus 로고
    • Why protein crystals favour some space-groups over others
    • Wukovitz S.W., Yeates T.O. Why protein crystals favour some space-groups over others. Nature Struct. Biol. 2:1995;1062-1067
    • (1995) Nature Struct. Biol , vol.2 , pp. 1062-1067
    • Wukovitz, S.W.1    Yeates, T.O.2
  • 47
    • 0027426789 scopus 로고
    • 2 with phosphonate transition-state analogues
    • 2 with phosphonate transition-state analogues. Biochemistry. 32:1993;10185-10192
    • (1993) Biochemistry , vol.32 , pp. 10185-10192
    • Yu, L.1    Dennis, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.