Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules

Nature

Volumn 425, Issue 6953, 2003, Pages 98-102

  Sung, Byung Je ^a   Hwang, Kwang Yeon ^a   Jeon, Young Ho ^a   Lee, Jae Il ^a   Heo, Yong Seok ^a   Kim, Jin Hwan ^a   Moon, Jinho ^a   Yoon, Jung Min ^a   Hyun, Young Lan ^a   Kim, Eunmi ^a   Eum, Sung Jin ^a   Park, Sam Yong ^b   Lee, Jie Oh ^c   Lee, Tae Gyu ^a   Ro, Seonggu ^a   Cho, Joong Myung ^a  

^a CrystalGenomics Inc   (South Korea)

^b YOKOHAMA CITY UNIVERSITY   (Japan)

^c Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION; DISEASE CONTROL; DRUG THERAPY; GENES; PHYSIOLOGY; TISSUE;

CATALYTIC DOMAINS;

ENZYMES;

PHOSPHODIESTERASE; PHOSPHODIESTERASE INHIBITOR; PHOSPHODIESTERASE V; SILDENAFIL; TADALAFIL; UNCLASSIFIED DRUG; VARDENAFIL;

MEDICINE;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; DRUG BINDING; ENZYME ACTIVE SITE; HUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING;

3',5'-CYCLIC-GMP PHOSPHODIESTERASE; BINDING SITES; CARBOLINES; CATALYTIC DOMAIN; HUMANS; HYDROGEN BONDING; IMIDAZOLES; MODELS, MOLECULAR; PHOSPHORIC DIESTER HYDROLASES; PIPERAZINES; PROTEIN CONFORMATION; SULFONES; TRIAZINES;

EID: 0041321268     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01914     Document Type: Article

References (23)

1. Beavo, J. A. Cyclic nucleotide phosphodiesterases: functional implications of multiple isoforms. Physiol. Rev. 75, 725-748 (1995).
2. Soderling, S. H. & Beavo, J. A. Regulation of cAMP and EGMP signaling: new phosphodiesterases and new functions. Curr. Opin. Cell Biol, 12, 174-179 (2000).
3. Corbin, J. D. & Francis, S. H. Cyclic GMP phosphodiesterase-5: target of sildenafil. J. Biol. Chem. 274, 13729-13732 (1999).
4. Rotella, D. P. Phosphodiestease 5 inhibitors: current status and potential application. Nature Rev. Drug Discov. 1, 674-682 (2002).
5. Conti, M., Nemoz, G., Sette, C. & Vicini, E. Recent progress in understanding the hormonal regulation of phosphodiesterases. Endocr. Rev. 16, 370-389 (1995).
6. Torphy, T. J. Phosphodiesterase isozymes. Am. J. Respir. Crit. Care Med. 157, 351-370 (1998).
7. Mechats, C., Andersen, C. B., Filopanti, M., Jin, S. L. & Conti, M. Cyclic nucleotide phosphodiesterases and their role in endocrine cell signaling. Trends Endocr. Met. 13, 29-35 (2002).
8. Xu, R. X. et al. Atomic structure of PDE4: Insights into phosphodiesterase mechanism and specificity. Science 288, 1822-1825 (2000).
9. Lee, M. E., Markowitz, J., Lee, J.-O. & Lee, H. Crystal structure of phosphodiesterase 4D and inhibitor complex. FEBS Lett. 530, 53-58 (2002).
10. Rybalkin, S. D., Rybalkina, I. G., Shimizu-Albergine, M., Tang, X. B. & Beavo, J. A. PDE5 is converted to an activated state upon cGMP binding to the GAF A domain. EMBO J. 23, 469-478 (2003).
11. Corbin, J. D. & Francis, S. H. Pharmacology of phosphodiesterase-5 inhibitors. Int. J. Clin. Pract. 56, 453-459 (2002).
12. Jeffrey, P. D. et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313-320 (1995).
13. Nikolov, D. B. et al. Crystal structure of a TFIIB-TBP-TATA-element ternary complex. Nature 377, 119-128 (1995).
14. Turko, I. V., Francis, S. H. & Corbin, J. D. Potential roles of conserved amino acids in the catalytic domain of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). J. Biol. Chem. 273, 6460-6466 (1998).
15. Young, J. M. Expert opinion: Vardenafil. Expert Opin. Invest. Drugs 11, 1487-1496 (2002).
16. Sekhar, K. R., Grondin, P., Francis, S. H. & Corbin, J. D. Phosphodiesterase Inhibitors (eds Schudt, C., Dent, G. & Rabe, K. F.) 135-146 (Academic, New York, 1996).
17. Doublie, S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-529 (1997).
18. Orme, M. W., Sawyer, J. S. & Schultze, L. M. Indole derivatives as PDE5-inhibitors. PCT Int. Appl. WO0236593 A1 (2002).
19. Otwinowski, M. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods. Enzymol. 276, 307-326 (1997).
20. Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D 55, 849-861 (1999).
21. Terwilliger, T. C. Maximum likelihood density modification. Acta Crystallogr. D 56, 965-972 (2000).
22. Jones, T., Zou, J.-Y., Cowan, S. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47,110-119 (1991).
23. Brûnger, A. T. et al. Crystallography & N.M.R. system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).