3b2r: Difference between revisions

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[[Image:3b2r.~~jpg~~|left|200px]]

[[Image:3b2r.png|left|200px]]

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~~'''~~Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil~~'''~~

===Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil===

~~==Overview==~~

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~~Vardenafil has higher affinity~~ to ~~phosphodiesterase-5~~ (~~PDE5~~) ~~than sildenafil and lower administered dosage for the treatment of erectile dysfunction. However~~, ~~the molecular basis for these differences is puzzling because two drugs have similar chemical structures. Reported here~~ is ~~a crystal structure of~~ the ~~fully active and nonmutated PDE5A1 catalytic domain in complex with vardenafil~~. ~~The structure shows that the conformation of the H~~-~~loop in the PDE5A1~~-vardenafil complex is different from those of any known structures of the unliganded PDE5 and its complexes with the inhibitors. In addition, the molecular configuration of vardenafil differs from that of sildenafil when bound to PDE5. It is noteworthy that the binding of vardenafil causes loss of the divalent metal ions that have been observed in all the previously published PDE structures. The conformational variation of both PDE5 and the inhibitors provides structural insight into the different potencies of the drugs.

The line below this paragraph, {{ABSTRACT_PUBMED_17959709}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17959709 is the PubMed ID number.

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==About this Structure==

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[[Category: Vardenafil]]

[[Category: Zinc]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu May 22~~ 21:48:51 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:53:29 2008''

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-[[Image:3b2r.jpg|left|200px]]
+{{Seed}}
+[[Image:3b2r.png|left|200px]]
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 {{STRUCTURE_3b2r|  PDB=3b2r  |  SCENE=  }}
-'''Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil'''
+===Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil===
-==Overview==
+<!--
-Vardenafil has higher affinity to phosphodiesterase-5 (PDE5) than sildenafil and lower administered dosage for the treatment of erectile dysfunction. However, the molecular basis for these differences is puzzling because two drugs have similar chemical structures. Reported here is a crystal structure of the fully active and nonmutated PDE5A1 catalytic domain in complex with vardenafil. The structure shows that the conformation of the H-loop in the PDE5A1-vardenafil complex is different from those of any known structures of the unliganded PDE5 and its complexes with the inhibitors. In addition, the molecular configuration of vardenafil differs from that of sildenafil when bound to PDE5. It is noteworthy that the binding of vardenafil causes loss of the divalent metal ions that have been observed in all the previously published PDE structures. The conformational variation of both PDE5 and the inhibitors provides structural insight into the different potencies of the drugs.
+The line below this paragraph, {{ABSTRACT_PUBMED_17959709}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17959709 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17959709}}
 ==About this Structure==
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 [[Category: Vardenafil]]
 [[Category: Zinc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 21:48:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:53:29 2008''