메뉴 건너뛰기




Volumn 48, Issue 23, 2005, Pages 7145-7152

Ligand docking in the gastric H+/K+-ATPase: Homology modeling of reversible inhibitor binding sites

Author keywords

[No Author keywords available]

Indexed keywords

1,2,3 TRIMETHYL 8 (PENTAFLUOROPHENYLMETHOXY)IMIDAZO[1,2 A]PYRIDINIUM IODIDE; 8 BENZYLOXY 2 METHYLIMIDAZO[1,2 A]PYRIDINE 3 ACETONITRILE; ADENOSINE TRIPHOSPHATASE (CALCIUM); HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; LANSOPRAZOLE; OMEPRAZOLE; PANTOPRAZOLE; PROTON PUMP INHIBITOR; UNCLASSIFIED DRUG;

EID: 28544439150     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050326o     Document Type: Article
Times cited : (18)

References (38)
  • 2
    • 0031448848 scopus 로고    scopus 로고
    • Changes in protein kinase C and adenylate cyclase in the temporal lobe from subjects with Schizophrenia
    • Dean, B.; Opeskin, K.; Pavey, G.; Hill, C.; Keks, N. Changes in Protein Kinase C and Adenylate Cyclase in the Temporal Lobe From Subjects With Schizophrenia. J. Neural Transm. 1997, 104 (11-12), 1371-1381.
    • (1997) J. Neural Transm. , vol.104 , Issue.11-12 , pp. 1371-1381
    • Dean, B.1    Opeskin, K.2    Pavey, G.3    Hill, C.4    Keks, N.5
  • 3
    • 0034041928 scopus 로고    scopus 로고
    • Reconstitution of the human 5-HT-(1D) receptor-G-protein coupling: Evidence for constitutive activity and multiple receptor conformations
    • Brys, R.; Josson, K.; Castelli, M. P.; Jurzak, M.; Lijnen, P.; Gommeren, W.; Leysen, J. Reconstitution of the Human 5-HT-(1D) Receptor-G-Protein Coupling: Evidence For Constitutive Activity and Multiple Receptor Conformations. Mol. Pharmacol. 2000, 57(6), 1132-1141.
    • (2000) Mol. Pharmacol. , vol.57 , Issue.6 , pp. 1132-1141
    • Brys, R.1    Josson, K.2    Castelli, M.P.3    Jurzak, M.4    Lijnen, P.5    Gommeren, W.6    Leysen, J.7
  • 4
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G-protein-coupled receptor kinases
    • Pronin, A. N.; Morris, A. J.; Surguchov, A.; Benovic, J. L. Synucleins Are a Novel Class of Substrates For G-Protein-Coupled Receptor Kinases. J. Biol. Chem. 2000, 275 (34), 26515-26522.
    • (2000) J. Biol. Chem. , vol.275 , Issue.34 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 6
    • 0021912737 scopus 로고
    • Structural relatedness of three ion-transport adenosine triphosphatases around their active sites of phosphorylation
    • Walderhaug, M. O.; Post, R. L.; Saccomani, G.; Leonard, R. T.; Briskin, D. P. Structural Relatedness of Three Ion-Transport Adenosine Triphosphatases Around Their Active Sites of Phosphorylation. J. Biol. Chem. 1985, 260 (6), 3852-3859.
    • (1985) J. Biol. Chem. , vol.260 , Issue.6 , pp. 3852-3859
    • Walderhaug, M.O.1    Post, R.L.2    Saccomani, G.3    Leonard, R.T.4    Briskin, D.P.5
  • 9
    • 0016156976 scopus 로고
    • An ATPase from dog gastric mucosa: Changes of outer pH in suspensions of membrane vesicles accompanying ATP hydrolysis
    • Lee, J.; Simpson, G.; Scholes, P. An ATPase From Dog Gastric Mucosa: Changes of Outer pH in Suspensions of Membrane Vesicles Accompanying ATP Hydrolysis. Biochem. Biophys. Res. Commun. 1974, 60 (2), 825-832.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , Issue.2 , pp. 825-832
    • Lee, J.1    Simpson, G.2    Scholes, P.3
  • 10
    • 0021984713 scopus 로고
    • Ion Transport Studies with H+-K+-ATPase-Rich Vesicles: Implications for HCl Secretion and Parietal Cell Physiology
    • Wolosin, J. M. Ion Transport Studies With H+-K+-ATPase-Rich Vesicles: Implications for HCl Secretion and Parietal Cell Physiology. Am. J. Physiol. 1985, 248 (6, Part 1), G595-607.
    • (1985) Am. J. Physiol. , vol.248 , Issue.6 PART 1
    • Wolosin, J.M.1
  • 11
  • 12
  • 13
    • 0034635518 scopus 로고    scopus 로고
    • Comparison of covalent with reversible inhibitor binding sites of the gastric H,K-ATPase by site-directed mutagenesis
    • Lambrecht, N.; Munson K.; Vagin O.; Sachs G. Comparison of Covalent With Reversible Inhibitor Binding Sites of the Gastric H,K-ATPase By Site-Directed Mutagenesis. J. Biol. Chem. 2000, 275 (6), 4041-4048.
    • (2000) J. Biol. Chem. , vol.275 , Issue.6 , pp. 4041-4048
    • Lambrecht, N.1    Munson, K.2    Vagin, O.3    Sachs, G.4
  • 14
    • 0029912849 scopus 로고    scopus 로고
    • Role of negatively charged residues in the fifth and sixth transmembrane domains of the catalytic subunit of gastric H+, K+-ATPase
    • Swarts, H. G.; Klaasse, C. H.; de Boer, M.; Fransen, A. M.; De Pont, J. J. Role of Negatively Charged Residues in the Fifth and Sixth Transmembrane Domains of the Catalytic Subunit of Gastric H+, K+-ATPase. J. Biol. Chem. 1996,271 (47), 29764-29772.
    • (1996) J. Biol. Chem. , vol.271 , Issue.47 , pp. 29764-29772
    • Swarts, H.G.1    Klaasse, C.H.2    De Boer, M.3    Fransen, A.M.4    De Pont, J.J.5
  • 15
    • 0030907484 scopus 로고    scopus 로고
    • Three-dimensional structure of the porcine gastric H,K-ATPase from negatively stained crystals
    • Xian, Y.; Hebert, H. Three-Dimensional Structure of the Porcine Gastric H,K-ATPase From Negatively Stained Crystals. J. Struct. Biol. 1997, 118 (3), 169-177.
    • (1997) J. Struct. Biol. , vol.118 , Issue.3 , pp. 169-177
    • Xian, Y.1    Hebert, H.2
  • 16
    • 0025287330 scopus 로고    scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine proteases
    • Greer, J. Comparative Modeling Methods: Application to the Family of the Mammalian Serine Proteases. Proteins 1999, 7, 317-334.
    • (1999) Proteins , vol.7 , pp. 317-334
    • Greer, J.1
  • 17
    • 0023305986 scopus 로고
    • Knowledge-based prediction of protein structures and the design of novel molecules
    • Blundell, T. L.; Sibanda B. L.; Sternberg, M. J. E.; Thornton, J. M. Knowledge-Based Prediction of Protein Structures and the Design of Novel Molecules. Nature 1987, 326, 347-352.
    • (1987) Nature , vol.326 , pp. 347-352
    • Blundell, T.L.1    Sibanda, B.L.2    Sternberg, M.J.E.3    Thornton, J.M.4
  • 18
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • Levitt, M. Accurate Modeling of Protein Conformation by Automatic Segment Matching. J. Mol. Biol. 1992, 226, 507-533.
    • (1992) J. Mol. Biol. , vol.226 , pp. 507-533
    • Levitt, M.1
  • 19
    • 0024395940 scopus 로고
    • A 3-D building blocks approach to analyzing and predicting structure of proteins
    • Unger, R.; Harel, D.; Wherland, S.; Sussman, J. L. A 3-D Building Blocks Approach to Analyzing and Predicting Structure of Proteins. Proteins 1989, 5, 355-373.
    • (1989) Proteins , vol.5 , pp. 355-373
    • Unger, R.1    Harel, D.2    Wherland, S.3    Sussman, J.L.4
  • 20
    • 0030322828 scopus 로고    scopus 로고
    • Homology modeling by distance geometry
    • Aszodi, A.; Taylor, W. R. Homology Modeling by Distance Geometry. Folding Des. 1996, 1, 325-334.
    • (1996) Folding des , vol.1 , pp. 325-334
    • Aszodi, A.1    Taylor, W.R.2
  • 21
    • 0027466730 scopus 로고
    • Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipolyated h protein from the pea leaf glycine cleavage system: A new automated method for the prediction of protein tertiary structure
    • Brocklehurst, S. M.; Perham, R. N. Prediction of the Three-Dimensional Structures of the Biotinylated Domain from Yeast Pyruvate Carboxylase and of the Lipolyated H Protein from the Pea Leaf Glycine Cleavage System: a New Automated Method for the Prediction of Protein Tertiary Structure. Protein Sci. 1993, 2, 629-639.
    • (1993) Protein Sci , vol.2 , pp. 629-639
    • Brocklehurst, S.M.1    Perham, R.N.2
  • 22
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial sestraints
    • Sali, Á.; Blundell, T. L. Comparative Protein Modelling by Satisfaction of Spatial Sestraints. J. Mol. Biol. 1993, 234 (3), 779-815.
    • (1993) J. Mol. Biol. , vol.234 , Issue.3 , pp. 779-815
    • Sali, Á.1    Blundell, T.L.2
  • 23
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C.; Nakasako M.; Nomura H.; Ogawa H. Crystal Structure of the Calcium Pump of Sarcoplasmic Reticulum at 2.6 Å Resolution. Nature 2000, 405 (8), 647-655.
    • (2000) Nature , vol.405 , Issue.8 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 24
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C.; Nomura, H. Structural Changes in the Calcium Pump Accompanying the Dissociation of Calcium. Nature 2002, 418 (8), 605-611.
    • (2002) Nature , vol.418 , Issue.8 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thornton, J. M. PROCHECK: a Program to Check the Stereochemical Quality of Protein Structures. J. Appl. Crystallogr. 1993, 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D.; Higgins, D. G.; Gibson, T. J. CLUSTAL W: Improving the Sensitivity of Progressive Multiple Sequence Alignment Through Sequence Weighting, Positions-Specific Gap Penalties and Weight Matrix Choice. Nucleic Acids Res. 1994, 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl, M. J. Recognition of Errors in Three-Dimensional Structures of Proteins. Proteins 1993, 17 (4), 355-362.
    • (1993) Proteins , vol.17 , Issue.4 , pp. 355-362
    • Sippl, M.J.1
  • 28
    • 0000009443 scopus 로고
    • Rapid comparison of protein structures
    • McLachlan, A. D. Rapid Comparison of Protein Structures. Acta Crystallogr. 1982, A38, 871-873.
    • (1982) Acta Crystallogr , vol.38 , pp. 871-873
    • McLachlan, A.D.1
  • 31
    • 0030748659 scopus 로고    scopus 로고
    • Mutational analysis of putative SCH 28080 binding sites of the gastric H+, K+-ATPase
    • Asano, S.; Matsuda, S.; Tega Y.; Shimizu, K.; Sakamoto, S.; Takeguchi N. Mutational Analysis of Putative SCH 28080 Binding Sites of the Gastric H+, K+-ATPase. J. Biol. Chem. 1997, 272 (28), 17668-17674.
    • (1997) J. Biol. Chem. , vol.272 , Issue.28 , pp. 17668-17674
    • Asano, S.1    Matsuda, S.2    Tega, Y.3    Shimizu, K.4    Sakamoto, S.5    Takeguchi, N.6
  • 32
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an emperical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated Docking Using a Lamarckian Genetic Algorithm and an Emperical Binding Free Energy Function. J. Comput. Chem. 1998, 19 (14), 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , Issue.14 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 34
    • 0034696579 scopus 로고    scopus 로고
    • Effects of mutations in M4 of the gastric H+, K+-ATPase on inhibition kinetics of SCH28080
    • Munson, K. B.; Lambrecht, N.; Sachs, G. Effects of mutations in M4 of the gastric H+, K+-ATPase on inhibition kinetics of SCH28080. Biochemistry 2000, 39 (11), 2997-3004.
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 2997-3004
    • Munson, K.B.1    Lambrecht, N.2    Sachs, G.3
  • 35
    • 0030930189 scopus 로고    scopus 로고
    • Sites of reaction of the gastric H,K-ATPase with extracytoplasmic thiol reagents
    • Besancon, M.; Simon, A.; Sachs, G.; Shin, J. M. Sites of Reaction of the Gastric H,K-ATPase with Extracytoplasmic Thiol Reagents. J. Biol. Chem. 1997, 272 (36), 22438-22446.
    • (1997) J. Biol. Chem. , vol.272 , Issue.36 , pp. 22438-22446
    • Besancon, M.1    Simon, A.2    Sachs, G.3    Shin, J.M.4
  • 36
    • 28544440488 scopus 로고    scopus 로고
    • +-competitive inhibitor SCH28080 provides tertiary structural information on the K transport domain of the H,K ATPase
    • +-Competitive Inhibitor SCH28080 Provides Tertiary Structural Information on the K Transport Domain of the H,K ATPase. Biophys. J. 2002, 82 (1), 1263.
    • (2002) Biophys. J. , vol.82 , Issue.1 , pp. 1263
    • Munson, K.1    Vagin, O.2    Sachs, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.