2paw

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{{STRUCTURE_2paw| PDB=2paw | SCENE= }}
{{STRUCTURE_2paw| PDB=2paw | SCENE= }}
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'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE'''
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===THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9521710 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9521710}}
==About this Structure==
==About this Structure==
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[[Category: Glycosyltransferase]]
[[Category: Glycosyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 08:08, 29 July 2008

Template:STRUCTURE 2paw

THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE

Template:ABSTRACT PUBMED 9521710

About this Structure

2PAW is a Single protein structure of sequence from Gallus gallus. This structure supersedes the now removed PDB entry 1paw. 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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