1dy8: Difference between revisions

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[[Image:1dy8.~~gif~~|left|200px]]

[[Image:1dy8.png|left|200px]]

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~~'''~~INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (INHIBITOR II)~~'''~~

===INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (INHIBITOR II)===

~~==Overview==~~

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The ~~hepatitis C virus NS3 protein contains a serine protease domain with a chymotrypsin-like fold~~, ~~which is a target for development of therapeutics. We report the crystal structures of this domain complexed with NS4A cofactor and with two potent~~, ~~reversible covalent inhibitors spanning~~ the ~~P1-P4 residues. Both inhibitors bind in an extended backbone conformation, forming an anti-parallel beta-sheet with one enzyme beta-strand. The P1 residue contributes most~~ to the ~~binding energy, whereas P2-P4 side chains are partially solvent exposed~~. ~~The structures do not show notable rearrangements of the active site upon inhibitor binding~~. ~~These results are significant for~~ the ~~development of antivirals~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10702283}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10702283 is the PubMed ID number.

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==About this Structure==

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[[Category: Protease inhibition]]

[[Category: Serine protease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 14~~:25:37 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:48:03 2008''

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-[[Image:1dy8.gif|left|200px]]
+{{Seed}}
+[[Image:1dy8.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dy8|  PDB=1dy8  |  SCENE=  }}
-'''INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (INHIBITOR II)'''
+===INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES (INHIBITOR II)===
-==Overview==
+<!--
-The hepatitis C virus NS3 protein contains a serine protease domain with a chymotrypsin-like fold, which is a target for development of therapeutics. We report the crystal structures of this domain complexed with NS4A cofactor and with two potent, reversible covalent inhibitors spanning the P1-P4 residues. Both inhibitors bind in an extended backbone conformation, forming an anti-parallel beta-sheet with one enzyme beta-strand. The P1 residue contributes most to the binding energy, whereas P2-P4 side chains are partially solvent exposed. The structures do not show notable rearrangements of the active site upon inhibitor binding. These results are significant for the development of antivirals.
+The line below this paragraph, {{ABSTRACT_PUBMED_10702283}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10702283 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10702283}}
 ==About this Structure==
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 [[Category: Protease inhibition]]
 [[Category: Serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:25:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:48:03 2008''