2paw
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(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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Revision as of 11:21, 21 November 2007
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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 superseeds 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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