P53R2: Difference between revisions
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Compare to the M2 subunit, these iron-binding sites are less efficient. This is due to the different conformations that the p53R2 subunit can adopt (stabilization or not of the two helix B and D). | Compare to the M2 subunit, these iron-binding sites are less efficient. This is due to the different conformations that the p53R2 subunit can adopt (stabilization or not of the two helix B and D). | ||
Furthermore the iron is the cofactor of the reaction catalyses by the RNR. The fact that in the p53R2 subunit the iron-binding is less efficient permits to imagine a specific anti-cancer therapy that targets these region, for example the drug [http://en.wikipedia.org/wiki/Deferoxamine deferoxamine mesylate] an iron chelator. Without iron, the reduction of the nucleotides can not take place and this could avoid the proliferation of cancer cells. | Furthermore the iron is the cofactor of the reaction catalyses by the RNR. The fact that in the p53R2 subunit the iron-binding is less efficient permits to imagine a specific anti-cancer therapy that targets these region, for example the drug [http://en.wikipedia.org/wiki/Deferoxamine deferoxamine mesylate] an iron chelator. Without iron, the reduction of the nucleotides can not take place and this could avoid the proliferation of cancer cells. | ||
=='''References'''== | |||
Publications : | |||
Smith P. et al, 2009, 2.6 A ° X-ray Crystal Structure of Human p53R2, a p53-Inducible Ribonucleotide Reductase. PMID: {{ABSTRACT_PUBMED_19728742}} | |||