Nitroreductase
From Proteopedia
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== Relevance == | == Relevance == | ||
| - | NR is of special interest due to its potential use as activator of prodrugs in cancer therapy<ref>PMID:26431849</ref>. | + | NR is of special interest due to its potential use as activator of prodrugs in cancer therapy<ref>PMID:26431849</ref>. |
== Structural highlights == | == Structural highlights == | ||
| - | NR cofactor FMN is bound to one subunit while the ligand - nicotinic acid - interacts with both subunits. | + | NR <scene name='48/489319/Cv/2'>cofactor FMN is bound directly to one subunit</scene> while the <scene name='48/489319/Cv/3'>ligand - nicotinic acid - interacts with both subunits</scene>. Water molecules shown as red spheres. |
</StructureSection> | </StructureSection> | ||
Revision as of 08:11, 31 May 2016
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3D structures of nitroreductase
Updated on 31-May-2016
References
- ↑ Lovering AL, Hyde EI, Searle PF, White SA. The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution. J Mol Biol. 2001 May 25;309(1):203-13. PMID:11491290 doi:10.1006/jmbi.2001.4653
- ↑ Williams EM, Little RF, Mowday AM, Rich MH, Chan-Hyams JV, Copp JN, Smaill JB, Patterson AV, Ackerley DF. Nitroreductase gene-directed enzyme prodrug therapy: insights and advances toward clinical utility. Biochem J. 2015 Oct 15;471(2):131-53. doi: 10.1042/BJ20150650. PMID:26431849 doi:http://dx.doi.org/10.1042/BJ20150650
