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Volumn 33, Issue 6, 2007, Pages 495-503

Binding mode analysis between membrane dipeptidase and its substrates

Author keywords

Cilastatin; Docking; Membrane dipeptidase (MDP); Pharmacophore; Virtual screening

Indexed keywords

CRYSTAL STRUCTURE; ENZYMES; LIGANDS; SUBSTRATES;

EID: 34548139739     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927020701236763     Document Type: Article
Times cited : (2)

References (32)
  • 2
    • 0033559556 scopus 로고    scopus 로고
    • This enzyme is also referred to as leukotriene-D4 hydrolase
    • I.J. White, J. Lawson, C.H. Williams, N.M. Hooper. This enzyme is also referred to as leukotriene-D4 hydrolase. Anal. Biochem., 268, 245 (1999).
    • (1999) Anal. Biochem , vol.268 , pp. 245
    • White, I.J.1    Lawson, J.2    Williams, C.H.3    Hooper, N.M.4
  • 3
    • 0033597209 scopus 로고    scopus 로고
    • Membrane dipeptidase is the receptor for a lung-targeting peptide identified by in vivo phage display
    • D. Rajotte, E.J. Ruoslahti. Membrane dipeptidase is the receptor for a lung-targeting peptide identified by in vivo phage display. J. Biol. Chem., 274, 11593 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 11593
    • Rajotte, D.1    Ruoslahti, E.J.2
  • 4
    • 0001105506 scopus 로고    scopus 로고
    • B.J. Campbell. Renal dipeptidase. Methods Enzymol., 19, 722 (1970).
    • B.J. Campbell. Renal dipeptidase. Methods Enzymol., 19, 722 (1970).
  • 6
    • 0019962519 scopus 로고
    • The tight binding and reversibility features have allowed cilastatin to be exploited in purification of MDP by affinity chromatography
    • H. Kropp, J.G. Sundelof, R. Hajdu, F.M. Kahan. The tight binding and reversibility features have allowed cilastatin to be exploited in purification of MDP by affinity chromatography. Antimicrob. Agents Chemother., 22, 62 (1982).
    • (1982) Antimicrob. Agents Chemother , vol.22 , pp. 62
    • Kropp, H.1    Sundelof, J.G.2    Hajdu, R.3    Kahan, F.M.4
  • 9
  • 10
    • 0029932458 scopus 로고    scopus 로고
    • Organ targeting in vivo using phage display peptide libraries
    • R. Pasqualini, E. Ruoslahti. Organ targeting in vivo using phage display peptide libraries. Nature, 380, 364 (1996).
    • (1996) Nature , vol.380 , pp. 364
    • Pasqualini, R.1    Ruoslahti, E.2
  • 12
    • 0032535999 scopus 로고    scopus 로고
    • Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model
    • W. Arap, R. Pasqualini, E. Ruoslahti. Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model. Science, 279, 377 (1998).
    • (1998) Science , vol.279 , pp. 377
    • Arap, W.1    Pasqualini, R.2    Ruoslahti, E.3
  • 13
    • 0030565784 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray investigation of a glycoprotein, human renal dipeptidase
    • Y. Nitanai, Y. Satow, H. Adachi, M. Tsujimoto. Crystallization and preliminary X-ray investigation of a glycoprotein, human renal dipeptidase. J. Cryst. Growth, 168, 280 (1996).
    • (1996) J. Cryst. Growth , vol.168 , pp. 280
    • Nitanai, Y.1    Satow, Y.2    Adachi, H.3    Tsujimoto, M.4
  • 14
    • 0036382767 scopus 로고    scopus 로고
    • Crystal structure of human renal dipeptidase involved in β-lactam hydrolysis
    • Y. Nitanai, Y. Satow, H. Adachi, M. Tsujimoto. Crystal structure of human renal dipeptidase involved in β-lactam hydrolysis. J. Mol. Biol., 321, 177 (2002).
    • (2002) J. Mol. Biol , vol.321 , pp. 177
    • Nitanai, Y.1    Satow, Y.2    Adachi, H.3    Tsujimoto, M.4
  • 15
    • 0037334067 scopus 로고    scopus 로고
    • A substrate variant as a high-affinity, reversible inhibitor: Insight from the X-ray structure of cilastatin bound to membrane dipeptidase
    • T.P. Smyth, J.G. Wall, Y. Nitanai. A substrate variant as a high-affinity, reversible inhibitor: insight from the X-ray structure of cilastatin bound to membrane dipeptidase. Bioorg. Med. Chem., 11, 991 (2003).
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 991
    • Smyth, T.P.1    Wall, J.G.2    Nitanai, Y.3
  • 16
    • 34548117258 scopus 로고    scopus 로고
    • Catalyst, Version 4.11, Accelrys, Inc, San Diego 2005
    • Catalyst, Version 4.11, Accelrys, Inc., San Diego (2005).
  • 17
    • 0037212102 scopus 로고    scopus 로고
    • LigandFit: A novel method for the shape-directed rapid docking of ligands to protein active sites
    • C.M. Venkatachalam, X. Jiang, T. Oldfield, M. Waldman. LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites. J. Mol. Graph. Model., 21, 289 (2003).
    • (2003) J. Mol. Graph. Model , vol.21 , pp. 289
    • Venkatachalam, C.M.1    Jiang, X.2    Oldfield, T.3    Waldman, M.4
  • 18
    • 34548110984 scopus 로고    scopus 로고
    • Discovery Studio, Version 1.5, Accelrys, Inc, San Diego 2006
    • Discovery Studio, Version 1.5, Accelrys, Inc., San Diego (2006).
  • 19
    • 18344382014 scopus 로고    scopus 로고
    • Comparative analysis of protein-bound ligand conformations with respect to catalyst's conformational space subsampling algorithms
    • J. Kirchmair, C. Laggner, G. Wolber, T. Langer. Comparative analysis of protein-bound ligand conformations with respect to catalyst's conformational space subsampling algorithms. J. Chem. Inf. Model., 45, 422 (2005).
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 422
    • Kirchmair, J.1    Laggner, C.2    Wolber, G.3    Langer, T.4
  • 20
    • 84966251980 scopus 로고
    • A family of variable-metric methods derived by variational means
    • D. Goldfarb. A family of variable-metric methods derived by variational means. Math. Comput., 24, 23 (1970).
    • (1970) Math. Comput , vol.24 , pp. 23
    • Goldfarb, D.1
  • 21
    • 19944366594 scopus 로고
    • The convergence of a class of double-rank minimization algorithms: 2. The new algorithm
    • C.G. Broyden. The convergence of a class of double-rank minimization algorithms: 2. The new algorithm. J. Inst. Math. Appl., 6, 222 (1970).
    • (1970) J. Inst. Math. Appl , vol.6 , pp. 222
    • Broyden, C.G.1
  • 24
    • 84986505839 scopus 로고
    • The effects of solvent screening in quantum mechanical calculations in protein systems
    • K. Baldridge, R. Fine, A. Hagler. The effects of solvent screening in quantum mechanical calculations in protein systems. J. Comput. Chem., 15, 1217 (1994).
    • (1994) J. Comput. Chem , vol.15 , pp. 1217
    • Baldridge, K.1    Fine, R.2    Hagler, A.3
  • 25
    • 0000072652 scopus 로고    scopus 로고
    • New combining rules for rare gas van der Waals parameters
    • M. Waldman, A.T. Hagler. New combining rules for rare gas van der Waals parameters. J. Comput. Chem., 14, 1077 (2003).
    • (2003) J. Comput. Chem , vol.14 , pp. 1077
    • Waldman, M.1    Hagler, A.T.2
  • 27
    • 0033545622 scopus 로고    scopus 로고
    • A general and fast scoring function for protein-ligand interactions: A simplified potential approach
    • I. Muegge, Y.C. Martin. A general and fast scoring function for protein-ligand interactions: a simplified potential approach. J. Med. Chem., 42, 791 (1999).
    • (1999) J. Med. Chem , vol.42 , pp. 791
    • Muegge, I.1    Martin, Y.C.2
  • 28
    • 0028454828 scopus 로고
    • The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure
    • H.J. Böhm. The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure. J. Comput. Aided Mol. Des., 8, 243 (1994).
    • (1994) J. Comput. Aided Mol. Des , vol.8 , pp. 243
    • Böhm, H.J.1
  • 29
    • 0028346359 scopus 로고
    • Directed mutagenesis of pig renal membrane dipeptidase His219 is critical but DHXXH motif is no essential for zinc binding or catalytic activity
    • S. Keynan, N.M. Hooper, A.J. Turner. Directed mutagenesis of pig renal membrane dipeptidase His219 is critical but DHXXH motif is no essential for zinc binding or catalytic activity. FEBS Lett., 349, 50 (1994).
    • (1994) FEBS Lett , vol.349 , pp. 50
    • Keynan, S.1    Hooper, N.M.2    Turner, A.J.3
  • 30
    • 3042829224 scopus 로고    scopus 로고
    • Substrate variants versus transition state analogues as noncovalent reversible enzyme inhibitors
    • T.P. Smyth. Substrate variants versus transition state analogues as noncovalent reversible enzyme inhibitors. Bioorg. Med. Chem., 12, 4081 (2004).
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 4081
    • Smyth, T.P.1
  • 32
    • 0030583724 scopus 로고    scopus 로고
    • Purification and kinetic properties of a D-amino-acid peptide hydrolyzing enzyme from pig kidney cortex and its tentative identification with renal membrane dipeptidase
    • T. Watanabe, Y. Kera, T. Matsumoto, R. Yamada. Purification and kinetic properties of a D-amino-acid peptide hydrolyzing enzyme from pig kidney cortex and its tentative identification with renal membrane dipeptidase. Biochim. Biophys. Acta, 1298, 109 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 109
    • Watanabe, T.1    Kera, Y.2    Matsumoto, T.3    Yamada, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.