1ed4: Difference between revisions

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[[Image:1ed4.~~gif~~|left|200px]]

[[Image:1ed4.png|left|200px]]

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~~'''~~BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE)~~'''~~

===BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE)===

~~==Overview==~~

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~~Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme~~-~~drug interactions are crucial for the development of potent, isoform~~-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, ~~S-isopropyl-isothiourea, and 2-aminothiazoline~~, ~~respectively. These structures reveal~~ the ~~importance of nonpolar van der Waals contacts in addition~~ to the ~~well-known hydrogen bonding interactions between inhibitor and enzyme~~. ~~The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in~~ the ~~NOS active site~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11051558}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11051558 is the PubMed ID number.

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==About this Structure==

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[[Category: Heme protein]]

[[Category: Nitric oxide synthase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 14~~:57~~:07~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:30:57 2008''

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-[[Image:1ed4.gif|left|200px]]
+{{Seed}}
+[[Image:1ed4.png|left|200px]]
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 {{STRUCTURE_1ed4|  PDB=1ed4  |  SCENE=  }}
-'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE)'''
+===BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE)===
-==Overview==
+<!--
-Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and 2-aminothiazoline, respectively. These structures reveal the importance of nonpolar van der Waals contacts in addition to the well-known hydrogen bonding interactions between inhibitor and enzyme. The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in the NOS active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_11051558}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11051558 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11051558}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Heme protein]]
 [[Category: Nitric oxide synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:57:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:30:57 2008''