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Volumn 59, Issue 1, 2016, Pages 282-293

Important Hydrogen Bond Networks in Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitor Design Revealed by Crystal Structures of Imidazoleisoindole Derivatives with IDO1

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXANE DERIVATIVE; HEME; IMIDAZOLE DERIVATIVE; INDOLEAMINE 2,3 DIOXYGENASE; INDOLEAMINE 2,3 DIOXYGENASE 1; INDOLEAMINE 2,3 DIOXYGENASE INHIBITOR; ISOINDOLE DERIVATIVE; UNCLASSIFIED DRUG; ENZYME INHIBITOR; INDOLEAMINE 2,3-DIOXYGENASE 1, HUMAN;

EID: 84955309574     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.5b01390     Document Type: Article
Times cited : (131)

References (50)
  • 1
    • 67649432744 scopus 로고    scopus 로고
    • Inhibitors of indoleamine-2,3-dioxygenase for cancer therapy: Can we see the wood for the trees?
    • Lob, S.; Konigsrainer, A.; Rammensee, H. G.; Opelz, G.; Terness, P. Inhibitors of indoleamine-2,3-dioxygenase for cancer therapy: can we see the wood for the trees? Nat. Rev. Cancer 2009, 9, 445-452 10.1038/nrc2639
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 445-452
    • Lob, S.1    Konigsrainer, A.2    Rammensee, H.G.3    Opelz, G.4    Terness, P.5
  • 2
    • 34248173331 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase and tumor-induced tolerance
    • Munn, D. H.; Mellor, A. L. Indoleamine 2,3-dioxygenase and tumor-induced tolerance J. Clin. Invest. 2007, 117, 1147-1154 10.1172/JCI31178
    • (2007) J. Clin. Invest. , vol.117 , pp. 1147-1154
    • Munn, D.H.1    Mellor, A.L.2
  • 3
    • 0034176031 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase production by human dendritic cells results in the inhibition of T cell proliferation
    • Hwu, P.; Du, M. X.; Lapointe, R.; Do, M.; Taylor, M. W.; Young, H. A. Indoleamine 2,3-dioxygenase production by human dendritic cells results in the inhibition of T cell proliferation J. Immunol. 2000, 164, 3596-3599 10.4049/jimmunol.164.7.3596
    • (2000) J. Immunol. , vol.164 , pp. 3596-3599
    • Hwu, P.1    Du, M.X.2    Lapointe, R.3    Do, M.4    Taylor, M.W.5    Young, H.A.6
  • 4
    • 63849112500 scopus 로고    scopus 로고
    • The role of indoleamine 2,3-dioxygenase in the induction of immune tolerance: Focus on hematology
    • Curti, A.; Trabanelli, S.; Salvestrini, V.; Baccarani, M.; Lemoli, R. M. The role of indoleamine 2,3-dioxygenase in the induction of immune tolerance: focus on hematology Blood 2009, 113, 2394-2401 10.1182/blood-2008-07-144485
    • (2009) Blood , vol.113 , pp. 2394-2401
    • Curti, A.1    Trabanelli, S.2    Salvestrini, V.3    Baccarani, M.4    Lemoli, R.M.5
  • 9
    • 84946425042 scopus 로고    scopus 로고
    • Challenges in the Discovery of Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitors
    • Rohrig, U. F.; Majjigapu, S. R.; Vogel, P.; Zoete, V.; Michielin, O. Challenges in the Discovery of Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitors J. Med. Chem. 2015, 10.1021/acs.jmedchem.5b00326
    • (2015) J. Med. Chem.
    • Rohrig, U.F.1    Majjigapu, S.R.2    Vogel, P.3    Zoete, V.4    Michielin, O.5
  • 10
    • 81755161497 scopus 로고    scopus 로고
    • Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors
    • Meininger, D.; Zalameda, L.; Liu, Y.; Stepan, L. P.; Borges, L.; McCarter, J. D.; Sutherland, C. L. Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors Biochim. Biophys. Acta, Proteins Proteomics 2011, 1814, 1947-1954 10.1016/j.bbapap.2011.07.023
    • (2011) Biochim. Biophys. Acta, Proteins Proteomics , vol.1814 , pp. 1947-1954
    • Meininger, D.1    Zalameda, L.2    Liu, Y.3    Stepan, L.P.4    Borges, L.5    McCarter, J.D.6    Sutherland, C.L.7
  • 12
    • 84990937835 scopus 로고    scopus 로고
    • IDO inhibitors move center stage in immuno-oncology
    • Sheridan, C. IDO inhibitors move center stage in immuno-oncology Nat. Biotechnol. 2015, 33, 321-322 10.1038/nbt0415-321
    • (2015) Nat. Biotechnol. , vol.33 , pp. 321-322
    • Sheridan, C.1
  • 14
    • 33644511372 scopus 로고    scopus 로고
    • Crystal structure of human indoleamine 2,3-dioxygenase: Catalytic mechanism of O2 incorporation by a heme-containing dioxygenase
    • Sugimoto, H.; Oda, S.; Otsuki, T.; Hino, T.; Yoshida, T.; Shiro, Y. Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase Proc. Natl. Acad. Sci. U. S. A. 2006, 103, 2611-2616 10.1073/pnas.0508996103
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2611-2616
    • Sugimoto, H.1    Oda, S.2    Otsuki, T.3    Hino, T.4    Yoshida, T.5    Shiro, Y.6
  • 15
    • 84907902924 scopus 로고    scopus 로고
    • Crystal Structures and Structure-Activity Relationships of Imidazothiazole Derivatives as IDO1 Inhibitors
    • Tojo, S.; Kohno, T.; Tanaka, T.; Kamioka, S.; Ota, Y.; Ishii, T.; Kamimoto, K.; Asano, S.; Isobe, Y. Crystal Structures and Structure-Activity Relationships of Imidazothiazole Derivatives as IDO1 Inhibitors ACS Med. Chem. Lett. 2014, 5, 1119-1123 10.1021/ml500247w
    • (2014) ACS Med. Chem. Lett. , vol.5 , pp. 1119-1123
    • Tojo, S.1    Kohno, T.2    Tanaka, T.3    Kamioka, S.4    Ota, Y.5    Ishii, T.6    Kamimoto, K.7    Asano, S.8    Isobe, Y.9
  • 16
    • 0024332546 scopus 로고
    • Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 1. Norharman and 4-phenylimidazole binding to the enzyme as inhibitors and heme ligands
    • Sono, M.; Cady, S. G. Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 1. Norharman and 4-phenylimidazole binding to the enzyme as inhibitors and heme ligands Biochemistry 1989, 28, 5392-5399 10.1021/bi00439a012
    • (1989) Biochemistry , vol.28 , pp. 5392-5399
    • Sono, M.1    Cady, S.G.2
  • 18
    • 84948808744 scopus 로고    scopus 로고
    • Challenges and Opportunities in the Discovery of New Therapeutics Targeting the Kynurenine Pathway
    • Dounay, A. B.; Tuttle, J. B.; Verhoest, P. R. Challenges and Opportunities in the Discovery of New Therapeutics Targeting the Kynurenine Pathway J. Med. Chem. 2015, 58, 8762-8782 10.1021/acs.jmedchem.5b00461
    • (2015) J. Med. Chem. , vol.58 , pp. 8762-8782
    • Dounay, A.B.1    Tuttle, J.B.2    Verhoest, P.R.3
  • 19
    • 0020478791 scopus 로고
    • Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme
    • Dawson, J. H.; Andersson, L. A.; Sono, M. Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme J. Biol. Chem. 1982, 257, 3606-3617
    • (1982) J. Biol. Chem. , vol.257 , pp. 3606-3617
    • Dawson, J.H.1    Andersson, L.A.2    Sono, M.3
  • 22
    • 0019381715 scopus 로고
    • Substrate interaction with cytochrome P-450
    • Schenkman, J. B.; Sligar, S. G.; Cinti, D. L. Substrate interaction with cytochrome P-450 Pharmacol. Ther. 1981, 12, 43-71 10.1016/0163-7258(81)90075-9
    • (1981) Pharmacol. Ther. , vol.12 , pp. 43-71
    • Schenkman, J.B.1    Sligar, S.G.2    Cinti, D.L.3
  • 23
    • 84955240266 scopus 로고    scopus 로고
    • Useful crystallographic terminology when utilising crystal structures
    • Hubbard, R. E. Royal Society of Chemistry: Cambridge, U.K
    • Brown, D. G.; Flocco, M. M. Useful crystallographic terminology when utilising crystal structures. In Structure-Based Drug Discovery: An Overview; Hubbard, R. E., Ed.; Royal Society of Chemistry: Cambridge, U.K., 2006; p 38.
    • (2006) Structure-Based Drug Discovery: An Overview , pp. 38
    • Brown, D.G.1    Flocco, M.M.2
  • 24
    • 84886586188 scopus 로고    scopus 로고
    • Protein crystallography for aspiring crystallographers or how to avoid pitfalls and traps in macromolecular structure determination
    • Wlodawer, A.; Minor, W.; Dauter, Z.; Jaskolski, M. Protein crystallography for aspiring crystallographers or how to avoid pitfalls and traps in macromolecular structure determination FEBS J. 2013, 280, 5705-5736 10.1111/febs.12495
    • (2013) FEBS J. , vol.280 , pp. 5705-5736
    • Wlodawer, A.1    Minor, W.2    Dauter, Z.3    Jaskolski, M.4
  • 25
    • 84943372312 scopus 로고    scopus 로고
    • Achieving High Quality Ligand Chemistry in Protein-Ligand Crystal Structures for Drug Design
    • Scapin, G. Patel, D. Arnold, E. Springer: Dordrecht, The Netherlands, DOI
    • Smart, O. S.; Bricogne, G. Achieving High Quality Ligand Chemistry in Protein-Ligand Crystal Structures for Drug Design. In Multifaceted Roles of Crystallography in Modern Drug Discovery; Scapin, G.; Patel, D.; Arnold, E., Eds.; Springer: Dordrecht, The Netherlands, 2015; pp 165-181, DOI: 10.1007/978-94-017-9719-1-13.
    • (2015) Multifaceted Roles of Crystallography in Modern Drug Discovery , pp. 165-181
    • Smart, O.S.1    Bricogne, G.2
  • 27
    • 66149100484 scopus 로고    scopus 로고
    • Screening of type i and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy
    • Das, A.; Zhao, J.; Schatz, G. C.; Sligar, S. G.; Van Duyne, R. P. Screening of type I and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy Anal. Chem. 2009, 81, 3754-3759 10.1021/ac802612z
    • (2009) Anal. Chem. , vol.81 , pp. 3754-3759
    • Das, A.1    Zhao, J.2    Schatz, G.C.3    Sligar, S.G.4    Van Duyne, R.P.5
  • 28
    • 33846928472 scopus 로고    scopus 로고
    • Preorganization in biological systems: Are conformational constraints worth the energy?
    • Martin, S. F. Preorganization in biological systems: Are conformational constraints worth the energy? Pure Appl. Chem. 2007, 79, 193-200 10.1351/pac200779020193
    • (2007) Pure Appl. Chem. , vol.79 , pp. 193-200
    • Martin, S.F.1
  • 31
    • 67650607734 scopus 로고    scopus 로고
    • The AZARYPHOS family of ligands for ambifunctional catalysis: Syntheses and use in ruthenium-catalyzed anti-Markovnikov hydration of terminal alkynes
    • Hintermann, L.; Dang, T. T.; Labonne, A.; Kribber, T.; Xiao, L.; Naumov, P. The AZARYPHOS family of ligands for ambifunctional catalysis: syntheses and use in ruthenium-catalyzed anti-Markovnikov hydration of terminal alkynes Chem.-Eur. J. 2009, 15, 7167-7179 10.1002/chem.200900563
    • (2009) Chem. - Eur. J. , vol.15 , pp. 7167-7179
    • Hintermann, L.1    Dang, T.T.2    Labonne, A.3    Kribber, T.4    Xiao, L.5    Naumov, P.6
  • 33
    • 77949799227 scopus 로고    scopus 로고
    • Intramolecular hydrogen bonding in medicinal chemistry
    • Kuhn, B.; Mohr, P.; Stahl, M. Intramolecular hydrogen bonding in medicinal chemistry J. Med. Chem. 2010, 53, 2601-2611 10.1021/jm100087s
    • (2010) J. Med. Chem. , vol.53 , pp. 2601-2611
    • Kuhn, B.1    Mohr, P.2    Stahl, M.3
  • 36
    • 0042510626 scopus 로고    scopus 로고
    • Identification of a new chemical class of potent angiogenesis inhibitors based on conformational considerations and database searching
    • Furet, P.; Bold, G.; Hofmann, F.; Manley, P.; Meyer, T.; Altmann, K. H. Identification of a new chemical class of potent angiogenesis inhibitors based on conformational considerations and database searching Bioorg. Med. Chem. Lett. 2003, 13, 2967-2971 10.1016/S0960-894X(03)00626-7
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2967-2971
    • Furet, P.1    Bold, G.2    Hofmann, F.3    Manley, P.4    Meyer, T.5    Altmann, K.H.6
  • 38
    • 0037413559 scopus 로고    scopus 로고
    • Discovery of a thieno[2,3-d]pyrimidine-2,4-dione bearing a p-methoxyureidophenyl moiety at the 6-position: A highly potent and orally bioavailable non-peptide antagonist for the human luteinizing hormone-releasing hormone receptor
    • Sasaki, S.; Cho, N.; Nara, Y.; Harada, M.; Endo, S.; Suzuki, N.; Furuya, S.; Fujino, M. Discovery of a thieno[2,3-d]pyrimidine-2,4-dione bearing a p-methoxyureidophenyl moiety at the 6-position: a highly potent and orally bioavailable non-peptide antagonist for the human luteinizing hormone-releasing hormone receptor J. Med. Chem. 2003, 46, 113-124 10.1021/jm020180i
    • (2003) J. Med. Chem. , vol.46 , pp. 113-124
    • Sasaki, S.1    Cho, N.2    Nara, Y.3    Harada, M.4    Endo, S.5    Suzuki, N.6    Furuya, S.7    Fujino, M.8
  • 39
    • 33750482579 scopus 로고    scopus 로고
    • Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: Successful in silico prediction of the relative permeabilities of cyclic peptides
    • Rezai, T.; Bock, J. E.; Zhou, M. V.; Kalyanaraman, C.; Lokey, R. S.; Jacobson, M. P. Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: successful in silico prediction of the relative permeabilities of cyclic peptides J. Am. Chem. Soc. 2006, 128, 14073-14080 10.1021/ja063076p
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14073-14080
    • Rezai, T.1    Bock, J.E.2    Zhou, M.V.3    Kalyanaraman, C.4    Lokey, R.S.5    Jacobson, M.P.6
  • 44
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A.; Teplyakov, A. MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 1997, 30, 1022-1025 10.1107/S0021889897006766
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50, 760-763 10.1107/S0907444994003112
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 47
    • 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.; Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr., Sect. A: Found. Crystallogr. 1991, 47, 110-119 10.1107/S0108767390010224
    • (1991) Acta Crystallogr., Sect. A: Found. Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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