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Volumn 337, Issue 2, 2004, Pages 355-365

Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with amp, 8-Br-AMP, and rolipram

Author keywords

8 Br AMP; AMP; CAMP, cyclic 3 ,5 adenosine monophosphate; CGMP, cyclic 3 ,5 gunosine monophosphate; ME2, metal ion 2; PDE; PDE, cyclic nucleotide phosphodiesterase; Rolipram; Structure

Indexed keywords

8 BROMO CYCLIC GMP; ADENOSINE PHOSPHATE; METAL ION; PHOSPHODIESTERASE IV; PHOSPHODIESTERASE IVB; ROLIPRAM; UNCLASSIFIED DRUG;

EID: 1442323778     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.01.040     Document Type: Article
Times cited : (116)

References (36)
  • 1
    • 0032605044 scopus 로고    scopus 로고
    • The molecular biology of cyclic nucleotide phosphodiesterases
    • Conti M., Jin S.L.C. The molecular biology of cyclic nucleotide phosphodiesterases. Prog. Nucl. Acid Res. Mol. Biol. 63:1999;1-38.
    • (1999) Prog. Nucl. Acid Res. Mol. Biol. , vol.63 , pp. 1-38
    • Conti, M.1    Jin, S.L.C.2
  • 2
    • 0031601339 scopus 로고    scopus 로고
    • The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: Intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions
    • Houslay M.D., Sullivan M., Bolger G.B. The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions. Advan. Pharmacol. 44:1998;225-342.
    • (1998) Advan. Pharmacol. , vol.44 , pp. 225-342
    • Houslay, M.D.1    Sullivan, M.2    Bolger, G.B.3
  • 4
    • 0039198237 scopus 로고    scopus 로고
    • Phosphodiesterase inhibitors
    • Torphy T.J. Phosphodiesterase inhibitors. Asthma. 2:1997;1755-1773.
    • (1997) Asthma , vol.2 , pp. 1755-1773
    • Torphy, T.J.1
  • 6
    • 0033015456 scopus 로고    scopus 로고
    • Isolation and characterization of PDE10A, a novel human 3′, 5′-cyclic nucleotide phosphodiesterase
    • Loughney K., Snyder P.B., Uher L., Rosman G.J., Ferguson K., Florio V.A. Isolation and characterization of PDE10A, a novel human 3′, 5′-cyclic nucleotide phosphodiesterase. Gene. 234:1999;109-117.
    • (1999) Gene , vol.234 , pp. 109-117
    • Loughney, K.1    Snyder, P.B.2    Uher, L.3    Rosman, G.J.4    Ferguson, K.5    Florio, V.A.6
  • 7
    • 0033572982 scopus 로고    scopus 로고
    • Striatum- and testis-specific phosphodiesterase PDE10A: Isolation and characterization of a rat PDE10A
    • Fujishige K., Kotera J., Omori K. Striatum- and testis-specific phosphodiesterase PDE10A: isolation and characterization of a rat PDE10A. Eur. J. Biochem. 266:1999;1118-1127.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1118-1127
    • Fujishige, K.1    Kotera, J.2    Omori, K.3
  • 9
    • 0030974622 scopus 로고    scopus 로고
    • Tailoring cAMP-signaling responses through isoform multiplicity
    • Houslay M.D., Milligan G. Tailoring cAMP-signaling responses through isoform multiplicity. Trends Biochem. Sci. 22:1997;217-224.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 217-224
    • Houslay, M.D.1    Milligan, G.2
  • 10
    • 0028802726 scopus 로고
    • Cyclic nucleotide phosphodiesterases: Functional implications of multiple isoforms
    • Beavo J.A. Cyclic nucleotide phosphodiesterases: functional implications of multiple isoforms. Physiol. Rev. 75:1995;725-748.
    • (1995) Physiol. Rev. , vol.75 , pp. 725-748
    • Beavo, J.A.1
  • 11
    • 0021941937 scopus 로고
    • A new generation of phosphodiesterase inhibitors: Multiple molecular forms of phosphodiesterase and the potential for drug selectivity
    • Weishaar R.E., Cain M.H., Bristol J.A. A new generation of phosphodiesterase inhibitors: multiple molecular forms of phosphodiesterase and the potential for drug selectivity. J. Med. Chem. 28:1985;537-545.
    • (1985) J. Med. Chem. , vol.28 , pp. 537-545
    • Weishaar, R.E.1    Cain, M.H.2    Bristol, J.A.3
  • 14
    • 0030702945 scopus 로고    scopus 로고
    • Human recombinant phosphodiesterase 4B2B binds (R)-rolipram at a single site with two affinities
    • Rocque W.J., Tian G., Wiseman J.S., Holmes W.D., Zajac-Thompson I., Willard D.H., et al. Human recombinant phosphodiesterase 4B2B binds (R) -rolipram at a single site with two affinities. Biochemistry. 36:1997;14250-14261.
    • (1997) Biochemistry , vol.36 , pp. 14250-14261
    • Rocque, W.J.1    Tian, G.2    Wiseman, J.S.3    Holmes, W.D.4    Zajac-Thompson, I.5    Willard, D.H.6
  • 15
    • 0034625541 scopus 로고    scopus 로고
    • Atomic structure of PDE4: Insights into phosphodiesterase mechanism and specificity
    • Xu R.X., Hassell A.M., Vanderwall D., Lambert M.H., Holmes W.D., Luther M.A., et al. Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity. Science. 288:2000;1822-1825.
    • (2000) Science , vol.288 , pp. 1822-1825
    • Xu, R.X.1    Hassell, A.M.2    Vanderwall, D.3    Lambert, M.H.4    Holmes, W.D.5    Luther, M.A.6
  • 16
    • 0037163858 scopus 로고    scopus 로고
    • Crystal structure of phosphodiesterase 4D and inhibitor complex
    • Lee M.E., Markowitz J., Lee J.-O., Lee H. Crystal structure of phosphodiesterase 4D and inhibitor complex. FEBS Letters. 530:2002;53-58.
    • (2002) FEBS Letters , vol.530 , pp. 53-58
    • Lee, M.E.1    Markowitz, J.2    Lee, J.-O.3    Lee, H.4
  • 17
    • 0038154006 scopus 로고    scopus 로고
    • Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity
    • Huai Q., Wang H., Sun Y., Kim H.-Y., Liu Y., Ke H. Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity. Structure. 11:2003;865-873.
    • (2003) Structure , vol.11 , pp. 865-873
    • Huai, Q.1    Wang, H.2    Sun, Y.3    Kim, H.-Y.4    Liu, Y.5    Ke, H.6
  • 18
    • 0242401840 scopus 로고    scopus 로고
    • The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis
    • Huai Q., Colicelli J., Ke H. The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis. Biochemistry. 42:2003;13220-13226.
    • (2003) Biochemistry , vol.42 , pp. 13220-13226
    • Huai, Q.1    Colicelli, J.2    Ke, H.3
  • 19
    • 0041321268 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules
    • Sung B.-J., Hwang K.-Y., Jeon Y.H., Lee J.I., Heo Y.-S., Kim J.H., et al. Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. Nature. 425:2003;98-102.
    • (2003) Nature , vol.425 , pp. 98-102
    • Sung, B.-J.1    Hwang, K.-Y.2    Jeon, Y.H.3    Lee, J.I.4    Heo, Y.-S.5    Kim, J.H.6
  • 20
    • 0031719432 scopus 로고    scopus 로고
    • Critical role of conserved histidine pairs HNXXH and HDXXH in recombinant human phosphodiesterase 4A
    • Omburo G.A., Jacobitz S., Torphy T.J., Colman R.W. Critical role of conserved histidine pairs HNXXH and HDXXH in recombinant human phosphodiesterase 4A. Cell. Signal. 10:1998;491-497.
    • (1998) Cell. Signal. , vol.10 , pp. 491-497
    • Omburo, G.A.1    Jacobitz, S.2    Torphy, T.J.3    Colman, R.W.4
  • 21
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzymology
    • Lipscomb W.N., Strater N. Recent advances in zinc enzymology. Chem. Rev. 96:1996;2375-2433.
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2433
    • Lipscomb, W.N.1    Strater, N.2
  • 22
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox D.E. Binuclear metallohydrolases. Chem. Rev. 96:1996;2435-2458.
    • (1996) Chem. Rev. , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 23
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden J.B., Phillips G.N., Neal T.M., Raushel F.M., Holden H.M. Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry. 40:2001;6989-6997.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips, G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 24
    • 0034801310 scopus 로고    scopus 로고
    • First computational evidence for a catalytic bridging hydroxide ion in a phosphodiesterase active site
    • Zhan C.-G., Zheng F. First computational evidence for a catalytic bridging hydroxide ion in a phosphodiesterase active site. J. Am. Chem. Soc. 123:2001;2835-2838.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2835-2838
    • Zhan, C.-G.1    Zheng, F.2
  • 25
    • 0015215169 scopus 로고
    • Chemical synthesis and biological activity of 8-substituted adenosine 3′,5′-cyclic monophosphate derivatives
    • Muneyama K., Bauer R.J., Shuman D.A., Robins R.K., Simon L.N. Chemical synthesis and biological activity of 8-substituted adenosine 3′,5′-cyclic monophosphate derivatives. Biochemistry. 10:1971;2390-2395.
    • (1971) Biochemistry , vol.10 , pp. 2390-2395
    • Muneyama, K.1    Bauer, R.J.2    Shuman, D.A.3    Robins, R.K.4    Simon, L.N.5
  • 26
    • 0015923811 scopus 로고
    • Effect of cyclic nucleotides on activity of cyclic 3′,5′- adenosine monophosphate phosphodiesterase
    • Harris D.N., Chasin M., Phillips M.B., Goldenberg H., Samaniego S., Hess S.M. Effect of cyclic nucleotides on activity of cyclic 3′,5′- adenosine monophosphate phosphodiesterase. Biochem. Pharmacol. 22:1973;221-228.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 221-228
    • Harris, D.N.1    Chasin, M.2    Phillips, M.B.3    Goldenberg, H.4    Samaniego, S.5    Hess, S.M.6
  • 27
    • 0026753496 scopus 로고
    • Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase. Mapping of the catalytic domain
    • Jin S.L.C., Swinnen J.V., Conti M. Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase. Mapping of the catalytic domain. J. Biol. Chem. 267:1992;18929-18939.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18929-18939
    • Jin, S.L.C.1    Swinnen, J.V.2    Conti, M.3
  • 28
    • 0027138677 scopus 로고
    • Use of a yeast expression system for the isolation and analysis of drug-resistant mutants of a mammalian phosphodiesterase
    • Pillai R., Kytle K., Reyes A., Colicelli J. Use of a yeast expression system for the isolation and analysis of drug-resistant mutants of a mammalian phosphodiesterase. Proc. Natl Acad. Sci. USA. 90:1993;11970-11974.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11970-11974
    • Pillai, R.1    Kytle, K.2    Reyes, A.3    Colicelli, J.4
  • 29
    • 0030981608 scopus 로고    scopus 로고
    • Role of conserved histidines in catalytic activity and inhibitor binding of human recombinant phosphodiesterase 4A
    • Jacobitz S., Ryan M.D., McLaughlin M.M., Livi G.P., DeWolf W.E., Torphy T.J. Role of conserved histidines in catalytic activity and inhibitor binding of human recombinant phosphodiesterase 4A. Mol. Pharmacol. 51:1997;999-1006.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 999-1006
    • Jacobitz, S.1    Ryan, M.D.2    McLaughlin, M.M.3    Livi, G.P.4    Dewolf, W.E.5    Torphy, T.J.6
  • 30
    • 0033582437 scopus 로고    scopus 로고
    • Identification of inhibitor specificity determinants in a mammalian phosphodiesterase
    • Atienza J.M., Susanto D., Huang C., McCarty A.S., Colicelli J. Identification of inhibitor specificity determinants in a mammalian phosphodiesterase. J. Biol. Chem. 274:1999;4839-4847.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4839-4847
    • Atienza, J.M.1    Susanto, D.2    Huang, C.3    McCarty, A.S.4    Colicelli, J.5
  • 31
    • 0035073963 scopus 로고    scopus 로고
    • Identification of inhibitor binding sites of the cAMP-specific phosphodiesterase 4
    • Richter W., Unciuleac L., Hermsdorf T., Kronbach T., Dettmer D. Identification of inhibitor binding sites of the cAMP-specific phosphodiesterase 4. Cell. Signal. 13:2001;287-297.
    • (2001) Cell. Signal. , vol.13 , pp. 287-297
    • Richter, W.1    Unciuleac, L.2    Hermsdorf, T.3    Kronbach, T.4    Dettmer, D.5
  • 32
    • 0031105672 scopus 로고    scopus 로고
    • Detailed characterization of a purified type 4 phosphodiesterase, HSPDE4B2B: Differentiation of high- and low-affinity (R)-rolipram binding
    • Rocque W.J., Holmes W.D., Patel I.R., Dougherty R.W., Ittoop O., Overton L., et al. Detailed characterization of a purified type 4 phosphodiesterase, HSPDE4B2B: differentiation of high- and low-affinity (R)-rolipram binding. Protein Expr. Purif. 9:1997;191-202.
    • (1997) Protein Expr. Purif. , vol.9 , pp. 191-202
    • Rocque, W.J.1    Holmes, W.D.2    Patel, I.R.3    Dougherty, R.W.4    Ittoop, O.5    Overton, L.6
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-776.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-776


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