Crystal structure of human ABAD/HSD10 with a bound inhibitor: Implications for design of Alzheimer's disease therapeutics

Journal of Molecular Biology

Volumn 342, Issue 3, 2004, Pages 943-952

  Kissinger, Charles R ^a   Rejto, Paul A ^a   Pelletier, Laura A ^a   Thomson, James A ^a   Showalter, Richard E ^a   Abreo, Melwyn A ^a   Agree, Charles S ^a   Margosiak, Stephen ^a   Meng, Jerry J ^a   Aust, Robert M ^a   Vanderpool, Darin ^a   Li, Bin ^a   Tempczyk Russell, Anna ^a   Villafranca, J Ernest ^a  

^a PFIZER INC   (United States)

Author keywords

ABAD; Alzheimer's disease; HSD10; short chain dehydrogenase

Indexed keywords

1 AZEPAN 1 YL 2 PHENYL 2 (4 THIOXO 1,4 DIHYDROPYRAZOLO[3,4 D]PYRIMIDIN 5 YL)ETHANONE; AG 18051; AMYLOID BETA PEPTIDE BINDING ALCOHOL DEHYDROGENASE; BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; OXIDOREDUCTASE INHIBITOR; TESTOSTERONE 17BETA DEHYDROGENASE; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG DESIGN; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HUMAN; MOLECULE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION;

EID: 4444231383     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.07.071     Document Type: Article

References (42)

1. D.J. Selkoe Normal and abnormal biology of the beta-amyloid precursor protein Annu. Rev. Neurosci. 17 1994 489 517
2. J. Hardy Amyloid, the presenilins and Alzheimer's disease Trends Neurosci. 20 1997 154 159
3. D.H. Small, and C.A. McLean Alzheimer's disease and the amyloid β protein: what is the role of amyloid? J. Neurochem. 73 1999 443 449
4. E. Storey, and R. Cappai The amyloid precursor protein of Alzheimer's disease and the Aβ peptide Neuropathol. Appl. Neurobiol. 25 1999 81 97
5. J. Kang, H.-G. Lemaire, A. Unterbeck, J.M. Salbaum, C.L. Masters, and K.H. Grzeschik The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor Nature 325 1987 733 736
6. C.A. Wilson, R.W. Doms, and V.M.-Y. Lee Intracellular APP processing and Aβ production in Alzheimer disease J. Neuropathol. Expt. Neurol. 58 1999 787 794
7. S.D. Yan, J. Fu, C. Soto, X. Chen, H. Zhu, and F. Al-Mohanna An intracellular protein that binds amyloid-b peptide and mediates neurotoxicity in Alzheimer's disease Nature 389 1997 689 695
8. X.-Y. He, H. Schulz, and S-Y. Yang A human brain L-3-hydroxyacyl-CoA dehydrogenase is identical to an amyloid β-peptide binding protein involved in Alzheimer's disease J. Biol. Chem. 273 1998 10741 10746
9. X.-Y. He, Y.-Z. Yang, H. Schultz, and S.-Y. Yang Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase Biochem. J. 345 2000 139 143
10. S.D. Yan, Y. Shi, A. Zhu, J. Fu, H. Zhu, and Y. Zhu Role of ERAB/L-3-hydroxyacyl-coenzyme A dehydrogenase type II activity in Aβ-induced cytotoxicity J. Biol. Chem. 274 1999 2145 2156
11. U.C.T. Oppermann, S. Salim, L.O. Tjernberg, L. Terenius, and H. Jörnvall Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease FEBS Letters 451 1999 238 242
12. A.J. Powell, J.A. Read, M.J. Banfield, F. Gunn-Moore, S.D. Yan, and J. Lustbader Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-β binding alcohol dehydrogenase (ABAD) J. Mol. Biol. 303 2000 311 327
13. X.-Y. He, G. Merz, P. Mehta, H. Schulz, and S.-Y. Yang Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme J. Biol. Chem. 274 1999 15014 15019
14. J. Lustbader, M. Cirilli, C. Lin, H.W. Xu, K. Takuma, and N. Wang ABAD-Aβ interaction is a direct link from Aβ to mitochondrial toxicity in Alzheimer's disease Science 16 2004 448 452
15. H. Jörnvall, B. Persson, M. Krook, S. Atrian, R. Gonzàlez-Duarte, J. Jeffrey, and D. Ghosh Short-chain dehydrogenase/reductases (SDR) Biochemistry 34 1995 6003 6013
16. M.G. Rossmann, A. Liljas, C.-I. Brändon, and L.J. Banaszak Evolutionary and structural relationships among dehydrogenases P.D. Boyer The Enzymes 1975 Academic Press New York 61 102
17. D. Ghosh, C.M. Weeks, P. Grochulski, W.L. Duax, M. Erman, R.L. Rimsay, and J.C. Orr Three-dimensional structure of holo 3α,20β- hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family Proc. Natl Acad. Sci. USA 88 1991 10064 10068
18. N. Tanaka, T. Nonaka, T. Tanabe, T. Yoshimoto, D. Tsuru, and Y. Mitsui Crystal structures of the binary and ternary complexes of 7α- hydroxysteroid dehydrogenase from Escherichia coli Biochemistry 35 1996 7715 7730
19. J. Benach, S. Atrian, R. Gonzáles-Duarte, and R. Laderstein The catalytic reaction and inhibitory mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 Å resolution by X-ray crystallography J. Mol. Biol. 289 1999 335 355
20. M. Hülsmeyer, H.-J. Hecht, K. Niefind, B. Hofer, L.D. Eltis, K.N. Timmis, and D. Schomburg Crystal structure of cis-biphenyl-2,3,dihydrodiol-2,3,- dehydrogenase from a PCB degrader at 2.0 Å resolution Protein Sci. 7 1998 1286 1293
21. J.S. McKinley-McGee, J.O. Winberg, and G. Pettersson Mechanism of action of Drosophila melanogaster alcohol dehydrogenase Biochem. J. 25 1991 879 885
22. D. Ghosh, V.Z. Pletnev, D.-W. Zhu, Z. Wawrzak, W.L. Duax, and W. Pangborn Structure of human estrogenic 17β-hydroxysteroid dehydrogenase at 2.20 Å resolution Structure 3 1995 503 513
23. K.B. Mullis, F. Faloona, S.J. Scharf, R.K. Saiki, G.T. Horn, and H.A. Erlich Specific enzymatic amplification of DNA in vitro: the polymerase chain reaction Cold Spring Harbor Symp. Quant. Biol. 51 1986 263 273
24. R.K. Saiki, D.H. Gelfand, S. Stoffel, S.J. Scharf, R. Higuchi, and G.T. Horn Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase Science 239 1988 487 491
25. C.C. Kan, M.R. Gehring, B.R. Nodes, C.A. Janson, R.J. Almassy, and Z. Hostomska Heterologous expression and purification of active human phosphoribosylglycinamide formyltransferase as a single domain J. Protein Chem. 11 1992 467 473
26. B.E. Schoner, R.M. Belagaje, and R.G. Schoner Translation of a synthetic two-cistron mRNA in Escherichia coli Proc. Natl Acad. Sci. USA 83 1986 8506 8510
27. T.A. Kunkel Rapid and efficient site-specific mutagenesis without phenotypic selection Proc. Natl Acad. Sci. USA 82 1985 488 492
28. B. Miroux, and J.E. Walker Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels J. Mol. Biol. 260 1996 289 298
29. S. Furuta, A. Kobayashi, S. Miyazawa, and T. Hashimoto Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria Biochim. Biophys. Acta 1350 1997 317 324
30. J.F. Binstock, and H. Shulz Fatty acid oxidation complex from Escherichia coli Methods Enzymol. 71 1981 403 411
31. Z. Otwinoski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
32. C.R. Kissinger, D.K. Gehlhaar, and D.B. Fogel Rapid automated molecular replacement by evolutionary search Acta Crystallog. sect. D 55 1999 484 491
33. A.T. Brünger XPLOR Manual, Version 3.1 1992 Yale University New Haven, CT
34. A.T. Brünger The free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 475
35. G.M. Sheldrick, and T.R. Schneider SHELX: High-resolution refinement Methods Enzymol. 277 1997 319 344
36. D.E. McRee A visual protein crystallographic software system for X11/Xview J. Mol. Graphics 10 1992 44 46
37. R. Engh, and R. Huber Accurate bond and angle parameters for X-ray protein-structure refinement Acta Crystallog. sect. A 47 1991 392 400
38. +-dependent 15-hydroxyprostaglandin dehydrogenase J. Biol. Chem. 265 1990 14888 14891
39. S.F. Altschul, T.L. Madden, A.A. Schäffer, J. Zhang, Z. Zhang, W. Miller, and D.J. Lipman Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucl. Acids Res. 25 1997 3389 3402
40. J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680
41. R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 283 291
42. A.C. Wallace, R.A. Laskowski, and J.M. Thorton LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8 1995 127 134