2pax: Difference between revisions

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[[Image:2pax.~~jpg~~|left|200px]]

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

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~~'''~~THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH 4-AMINO-1,8-NAPHTHALIMIDE~~'''~~

===THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH 4-AMINO-1,8-NAPHTHALIMIDE===

~~==Overview==~~

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~~Inhibitors of poly(ADP-ribose) polymerase (PARP~~, EC 2.4.2.30) are of clinical interest because they have potential for improving radiation therapy and chemotherapy of cancer. The refined binding structures of four such inhibitors are reported together with the ~~refined structure of~~ the ~~unligated catalytic fragment of the enzyme~~. ~~Following their design, all inhibitors bind at the position of the nicotinamide moiety of the substrate NAD+~~. ~~The observed binding mode suggests inhibitor improvements that avoid other NAD(+~~)~~-binding enzymes. Because the binding pocket of NAD+ has been strongly conserved during evolution, the homology with ADP-ribosylating bacterial toxins could be used to extend the bound nicotinamide~~, ~~which~~ is ~~marked by the inhibitors, to~~ the ~~full NAD+ molecule~~.

The line below this paragraph, {{ABSTRACT_PUBMED_9521710}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9521710 is the PubMed ID number.

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==About this Structure==

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[[Category: Glycosyltransferase]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 12~~:45:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:11:01 2008''

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-[[Image:2pax.jpg|left|200px]]
+{{Seed}}
+[[Image:2pax.png|left|200px]]
 <!--
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 {{STRUCTURE_2pax|  PDB=2pax  |  SCENE=  }}
-'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH 4-AMINO-1,8-NAPHTHALIMIDE'''
+===THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH 4-AMINO-1,8-NAPHTHALIMIDE===
-==Overview==
+<!--
-Inhibitors of poly(ADP-ribose) polymerase (PARP, EC 2.4.2.30) are of clinical interest because they have potential for improving radiation therapy and chemotherapy of cancer. The refined binding structures of four such inhibitors are reported together with the refined structure of the unligated catalytic fragment of the enzyme. Following their design, all inhibitors bind at the position of the nicotinamide moiety of the substrate NAD+. The observed binding mode suggests inhibitor improvements that avoid other NAD(+)-binding enzymes. Because the binding pocket of NAD+ has been strongly conserved during evolution, the homology with ADP-ribosylating bacterial toxins could be used to extend the bound nicotinamide, which is marked by the inhibitors, to the full NAD+ molecule.
+The line below this paragraph, {{ABSTRACT_PUBMED_9521710}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9521710 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9521710}}
 ==About this Structure==
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 [[Category: Glycosyltransferase]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:45:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:11:01 2008''