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Volumn 289, Issue 12, 2014, Pages 8562-8569

The structure of human 15-lipoxygenase-2 with a substrate mimic

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS;

EID: 84897017271     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.543777     Document Type: Article
Times cited : (106)

References (36)
  • 1
    • 0033812812 scopus 로고    scopus 로고
    • Overexpression of 15-lipoxygenase in vascular endothelium accelerates early atherosclerosis in LDL receptor-deficient mice
    • Harats, D., Shaish, A., George, J., Mulkins, M., Kurihara, H., Levkovitz, H., and Sigal, E. (2000) Overexpression of 15-lipoxygenase in vascular endothelium accelerates early atherosclerosis in LDL receptor-deficient mice. Arterioscler. Thromb. Vasc. Biol. 20, 2100-2105
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2100-2105
    • Harats, D.1    Shaish, A.2    George, J.3    Mulkins, M.4    Kurihara, H.5    Levkovitz, H.6    Sigal, E.7
  • 2
    • 8244253670 scopus 로고    scopus 로고
    • Attenuation of diet-induced atherosclerosis in rabbits with a highly selective 15-lipoxygenase inhibitor lacking significant antioxidant properties
    • DOI 10.1038/sj.bjp.0701007
    • Sendobry, S. M., Cornicelli, J. A., Welch, K., Bocan, T., Tait, B., Trivedi, B. K., Colbry, N., Dyer, R. D., Feinmark, S. J., and Daugherty, A. (1997) Attenuation of diet-induced atherosclerosis in rabbits with a highly selective 15-lipoxygenase inhibitor lacking significant antioxidant properties. Br. J. Pharmacol. 120, 1199-1206 (Pubitemid 27149668)
    • (1997) British Journal of Pharmacology , vol.120 , Issue.7 , pp. 1199-1206
    • Sendobry, S.M.1    Cornicelli, J.A.2    Welch, K.3    Bocan, T.4    Tait, B.5    Trivedi, B.K.6    Colbry, N.7    Dyer, R.D.8    Feinmark, S.J.9    Daugherty, A.10
  • 3
    • 0032006236 scopus 로고    scopus 로고
    • A specific 15-lipoxygenase inhibitor limits the progression and monocyte-macrophage enrichment of hypercholesterolemia-induced atherosclerosis in the rabbit
    • DOI 10.1016/S0021-9150(97)00204-9, PII S0021915097002049
    • Bocan, T. M., Rosebury, W. S., Mueller, S. B., Kuchera, S., Welch, K., Daugherty, A., and Cornicelli, J. A. (1998) A specific 15-lipoxygenase inhibitor limits the progression and monocyte-macrophage enrichment of hypercholesterolemia-induced atherosclerosis in the rabbit. Atherosclerosis 136, 203-216 (Pubitemid 28133408)
    • (1998) Atherosclerosis , vol.136 , Issue.2 , pp. 203-216
    • Bocan, T.M.A.1    Rosebury, W.S.2    Mueller, S.B.3    Susan, K.4    Welch, K.5    Daugherty, A.6    Cornicelli, J.A.7
  • 4
    • 17144453406 scopus 로고    scopus 로고
    • Lipoxygenase genes and their targeted disruption
    • DOI 10.1016/S0090-6980(02)00036-9, PII S0090698002000369
    • Funk, C. D., Chen, X. S., Johnson, E. N., and Zhao, L. (2002) Lipoxygenase genes and their targeted disruption. Prostaglandins Other Lipid. Mediat. 68, 303-312 (Pubitemid 35247403)
    • (2002) Prostaglandins and Other Lipid Mediators , vol.68-69 , pp. 303-312
    • Funk, C.D.1    Chen, X.-S.2    Johnson, E.N.3    Zhao, L.4
  • 5
    • 33745030151 scopus 로고    scopus 로고
    • Lipoxygenase pathways as mediators of early inflammatory events in atherosclerosis
    • Funk, C. D. (2006) Lipoxygenase pathways as mediators of early inflammatory events in atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 26, 1204-1206
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 1204-1206
    • Funk, C.D.1
  • 7
    • 84867884637 scopus 로고    scopus 로고
    • Expression and regulation of 12/15-lipoxygenases in human primary macrophages
    • Wuest, S. J., Crucet, M., Gemperle, C., Loretz, C., and Hersberger, M. (2012) Expression and regulation of 12/15-lipoxygenases in human primary macrophages. Atherosclerosis 225, 121-127
    • (2012) Atherosclerosis , vol.225 , pp. 121-127
    • Wuest, S.J.1    Crucet, M.2    Gemperle, C.3    Loretz, C.4    Hersberger, M.5
  • 8
  • 9
    • 84885805852 scopus 로고    scopus 로고
    • The transcription factor CREB enhances interleukin-17A production and inflammation in a mouse model of atherosclerosis
    • Kotla, S., Singh, N. K., Heckle, M. R., Tigyi, G. J., and Rao, G. N. (2013) The transcription factor CREB enhances interleukin-17A production and inflammation in a mouse model of atherosclerosis. Sci. Signal. 6, ra83
    • (2013) Sci. Signal. , vol.6
    • Kotla, S.1    Singh, N.K.2    Heckle, M.R.3    Tigyi, G.J.4    Rao, G.N.5
  • 10
    • 0033588022 scopus 로고    scopus 로고
    • Lipoxygenases: Occurrence, functions, catalysis, and acquisition of substrate
    • Brash, A. R. (1999) Lipoxygenases: occurrence, functions, catalysis, and acquisition of substrate. J. Biol. Chem. 274, 23679-23682
    • (1999) J. Biol. Chem. , vol.274 , pp. 23679-23682
    • Brash, A.R.1
  • 11
    • 80054857565 scopus 로고    scopus 로고
    • Endogenous signaling by omega-3 docosahexaenoic acid-derived mediators sustains homeostatic synaptic and circuitry integrity
    • Bazan, N. G., Musto, A. E., and Knott, E. J. (2011) Endogenous signaling by omega-3 docosahexaenoic acid-derived mediators sustains homeostatic synaptic and circuitry integrity. Mol. Neurobiol. 44, 216-222
    • (2011) Mol. Neurobiol. , vol.44 , pp. 216-222
    • Bazan, N.G.1    Musto, A.E.2    Knott, E.J.3
  • 12
    • 0027246677 scopus 로고
    • The three-dimensional structure of an arachidonic acid 15-lipoxygenase
    • Boyington, J. C., Gaffney, B. J., and Amzel, L. M. (1993) The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science 260, 1482-1486 (Pubitemid 23273261)
    • (1993) Science , vol.260 , Issue.5113 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 13
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • (Carter, C. W., and Sweet, R. M., eds) Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode in Methods Enzymology (Carter, C. W., and Sweet, R. M., eds) pp. 307-326, Academic Press, New York
    • (1997) Methods Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63, 103-138
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 17
    • 34250854730 scopus 로고    scopus 로고
    • Using Nanodiscs to Create Water-Soluble Transmembrane Chemoreceptors Inserted in Lipid Bilayers
    • DOI 10.1016/S0076-6879(07)23014-9, PII S0076687907230149, Two Component Signaling Systems, Part B
    • Boldog, T., Li, M., and Hazelbauer, G. L. (2007) Using Nanodiscs to create water-soluble transmembrane chemoreceptors inserted in lipid bilayers. Methods Enzymol. 423, 317-335 (Pubitemid 46991102)
    • (2007) Methods in Enzymology , vol.423 , pp. 317-335
    • Boldog, T.1    Li, M.2    Hazelbauer, G.L.3
  • 18
    • 1642382983 scopus 로고    scopus 로고
    • Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
    • DOI 10.1021/ja0393574
    • Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., and Sligar, S. G. (2004) Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size. J. Am. Chem. Soc. 126, 3477-3487 (Pubitemid 38366738)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.11 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 20
    • 38549129314 scopus 로고    scopus 로고
    • Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data
    • DOI 10.1002/prot.21590
    • Choi, J., Chon, J. K., Kim, S., and Shin, W. (2008) Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data. Proteins 70, 1023-1032 (Pubitemid 351161958)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.3 , pp. 1023-1032
    • Choi, J.1    Jae, K.C.2    Kim, S.3    Shin, W.4
  • 21
    • 84865800398 scopus 로고    scopus 로고
    • Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis
    • Xu, S., Mueser, T. C., Marnett, L. J., and Funk, M. O., Jr. (2012) Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis. Structure 20, 1490-1497
    • (2012) Structure , vol.20 , pp. 1490-1497
    • Xu, S.1    Mueser, T.C.2    Marnett, L.J.3    Funk Jr., M.O.4
  • 23
    • 69049086852 scopus 로고    scopus 로고
    • The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity
    • Neau, D. B., Gilbert, N. C., Bartlett, S. G., Boeglin, W., Brash, A. R., and Newcomer, M. E. (2009) The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity. Biochemistry 48, 7906-7915
    • (2009) Biochemistry , vol.48 , pp. 7906-7915
    • Neau, D.B.1    Gilbert, N.C.2    Bartlett, S.G.3    Boeglin, W.4    Brash, A.R.5    Newcomer, M.E.6
  • 24
    • 0027246677 scopus 로고
    • The three-dimensional structure of an arachidonic acid 15-lipoxygenase
    • Boyington, J. C., Gaffney, B. J., and Amzel, L. M. (1993) The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science 260, 1482-1486 (Pubitemid 23273261)
    • (1993) Science , vol.260 , Issue.5113 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 25
    • 0034624019 scopus 로고    scopus 로고
    • The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity
    • DOI 10.1074/jbc.M006136200
    • Hammarberg, T., Provost, P., Persson, B., and Rådmark, O. (2000) The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity. J. Biol. Chem. 275, 38787-38793 (Pubitemid 32009215)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38787-38793
    • Hammarberg, T.1    Provost, P.2    Persson, B.3    Radmark, O.4
  • 26
    • 0037066761 scopus 로고    scopus 로고
    • Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase
    • DOI 10.1074/jbc.M112393200
    • Kulkarni, S., Das, S., Funk, C. D., Murray, D., and Cho, W. (2002) Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase. J. Biol. Chem. 277, 13167-13174 (Pubitemid 34952687)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13167-13174
    • Kulkarni, S.1    Das, S.2    Funk, C.D.3    Murray, D.4    Cho, W.5
  • 27
    • 0033571064 scopus 로고    scopus 로고
    • Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase
    • Kilty, I., Logan, A., and Vickers, P. J. (1999) Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase. Eur. J. Biochem. 266, 83-93
    • (1999) Eur. J. Biochem. , vol.266 , pp. 83-93
    • Kilty, I.1    Logan, A.2    Vickers, P.J.3
  • 28
    • 34248596797 scopus 로고    scopus 로고
    • Control of Oxygenation in Lipoxygenase and Cyclooxygenase Catalysis
    • DOI 10.1016/j.chembiol.2007.04.007, PII S1074552107001457
    • Schneider, C., Pratt, D. A., Porter, N. A., and Brash, A. R. (2007) Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. Chem. Biol. 14, 473-488 (Pubitemid 46765155)
    • (2007) Chemistry and Biology , vol.14 , Issue.5 , pp. 473-488
    • Schneider, C.1    Pratt, D.A.2    Porter, N.A.3    Brash, A.R.4
  • 29
    • 34547426963 scopus 로고    scopus 로고
    • Biosynthesis and metabolism of leukotrienes
    • DOI 10.1042/BJ20070289
    • Murphy, R. C., and Gijón, M. A. (2007) Biosynthesis and metabolism of leukotrienes. Biochem. J. 405, 379-395 (Pubitemid 47172035)
    • (2007) Biochemical Journal , vol.405 , Issue.3 , pp. 379-395
    • Murphy, R.C.1    Gijon, M.A.2
  • 30
    • 0034811728 scopus 로고    scopus 로고
    • Steric control of oxygenation regiochemistry in soybean lipoxygenase-1
    • DOI 10.1021/ja003855k
    • Knapp, M. J., Seebeck, F. P., and Klinman, J. P. (2001) Steric control of oxygenation regiochemistry in soybean lipoxygenase-1. J. Am. Chem. Soc. 123, 2931-2932 (Pubitemid 32910739)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.12 , pp. 2931-2932
    • Knapp, M.J.1    Seebeck, F.P.2    Klinman, J.P.3
  • 31
    • 8144220042 scopus 로고    scopus 로고
    • A single active site residue directs oxygenation stereospecificity in lipoxygenases: Stereocontrol is linked to the position of oxygenation
    • Coffa, G., and Brash, A. R. (2004) A single active site residue directs oxygenation stereospecificity in lipoxygenases: Stereocontrol is linked to the position of oxygenation. Proc. Natl. Acad. Sci. U.S.A.
    • (2004) Proc. Natl. Acad. Sci. U.S.A.
    • Coffa, G.1    Brash, A.R.2
  • 32
    • 84863794133 scopus 로고    scopus 로고
    • Cholesteryl ester acyl oxidation and remodeling in murine macrophages: Formation of oxidized phosphatidylcholine
    • Hutchins, P. M., and Murphy, R. C. (2012) Cholesteryl ester acyl oxidation and remodeling in murine macrophages: formation of oxidized phosphatidylcholine. J. Lipid Res. 53, 1588-1597
    • (2012) J. Lipid Res. , vol.53 , pp. 1588-1597
    • Hutchins, P.M.1    Murphy, R.C.2
  • 36
    • 0033966938 scopus 로고    scopus 로고
    • Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2
    • DOI 10.1074/jbc.275.2.1287
    • Jisaka, M., Kim, R. B., Boeglin, W. E., and Brash, A. R. (2000) Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2. J. Biol. Chem. 275, 1287-1293 (Pubitemid 30051183)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 1287-1293
    • Jisaka, M.1    Kim, R.B.2    Boeglin, W.E.3    Brash, A.R.4


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