2c4w: Difference between revisions

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[[Image:2c4w.~~gif~~|left|200px]]

[[Image:2c4w.png|left|200px]]

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~~'''~~TYPE II DEHYDROQUINASE FROM H. PYLORI IN COMPLEX WITH AH9095~~'''~~

===TYPE II DEHYDROQUINASE FROM H. PYLORI IN COMPLEX WITH AH9095===

~~==Overview==~~

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The ~~crystal structures of~~ the ~~type II dehydroquinase~~ (~~DHQase) from Helicobacter pylori in complex with three competitive inhibitors have been determined~~. ~~The inhibitors are the substrate analogue 2,3-anhydroquinate (FA1), citrate, and an oxoxanthene sulfonamide derivative (AH9095~~)~~. Despite the very different chemical nature of the inhibitors~~, ~~in each case the primary point of interaction with the enzyme~~ is ~~via~~ the ~~residues that bind the C1 functionalities of the substrate, 3~~-~~dehydroquinate, i.e., N76, H102, I103, and H104. The DHQase/AH9095 complex crystal structure shows that sulfonamides can form a scaffold for nonsubstrate~~-~~like inhibitors and identifies a large conserved hydrophobic patch at the entrance to the active site as a locus that can be exploited in the development of new ligands.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16480265}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16480265 is the PubMed ID number.

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==About this Structure==

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[[Category: Shikimate pathway]]

[[Category: Sulphonamide]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 21~~:15:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:32:12 2008''

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-[[Image:2c4w.gif|left|200px]]
+{{Seed}}
+[[Image:2c4w.png|left|200px]]
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 {{STRUCTURE_2c4w|  PDB=2c4w  |  SCENE=  }}
-'''TYPE II DEHYDROQUINASE FROM H. PYLORI IN COMPLEX WITH AH9095'''
+===TYPE II DEHYDROQUINASE FROM H. PYLORI IN COMPLEX WITH AH9095===
-==Overview==
+<!--
-The crystal structures of the type II dehydroquinase (DHQase) from Helicobacter pylori in complex with three competitive inhibitors have been determined. The inhibitors are the substrate analogue 2,3-anhydroquinate (FA1), citrate, and an oxoxanthene sulfonamide derivative (AH9095). Despite the very different chemical nature of the inhibitors, in each case the primary point of interaction with the enzyme is via the residues that bind the C1 functionalities of the substrate, 3-dehydroquinate, i.e., N76, H102, I103, and H104. The DHQase/AH9095 complex crystal structure shows that sulfonamides can form a scaffold for nonsubstrate-like inhibitors and identifies a large conserved hydrophobic patch at the entrance to the active site as a locus that can be exploited in the development of new ligands.
+The line below this paragraph, {{ABSTRACT_PUBMED_16480265}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16480265 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16480265}}
 ==About this Structure==
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 [[Category: Shikimate pathway]]
 [[Category: Sulphonamide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:15:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:32:12 2008''