2paw
From Proteopedia
(New page: 200px<br /><applet load="2paw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2paw, resolution 2.3Å" /> '''THE CATALYTIC FRAGMEN...) |
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| - | [[Image:2paw.gif|left|200px]]<br /><applet load="2paw" size=" | + | [[Image:2paw.gif|left|200px]]<br /><applet load="2paw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2paw, resolution 2.3Å" /> | caption="2paw, resolution 2.3Å" /> | ||
'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE'''<br /> | '''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Inhibitors of poly(ADP-ribose) polymerase (PARP, EC 2.4.2.30) are of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2PAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure | + | 2PAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry 1PAW. Active as [http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PAW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ruf, A.]] | [[Category: Ruf, A.]] | ||
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
[[Category: glycosyltransferase]] | [[Category: glycosyltransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:27:46 2008'' |
Revision as of 16:28, 21 February 2008
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THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE
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.
About this Structure
2PAW is a Single protein structure of sequence from Gallus gallus. This structure supersedes the now removed PDB entry 1PAW. Active as NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30 Full crystallographic information is available from OCA.
Reference
Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling., Ruf A, de Murcia G, Schulz GE, Biochemistry. 1998 Mar 17;37(11):3893-900. PMID:9521710
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