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| ==NMR Structure of RCL in complex with GMP== | | ==NMR Structure of RCL in complex with GMP== |
- | <StructureSection load='2klh' size='340' side='right'caption='[[2klh]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2klh' size='340' side='right'caption='[[2klh]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2klh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KLH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2klh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KLH FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rcl ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2klh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klh OCA], [https://pdbe.org/2klh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2klh RCSB], [https://www.ebi.ac.uk/pdbsum/2klh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2klh ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2klh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klh OCA], [https://pdbe.org/2klh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2klh RCSB], [https://www.ebi.ac.uk/pdbsum/2klh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2klh ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/DNPH1_RAT DNPH1_RAT]] Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.<ref>PMID:17234634</ref>
| + | [https://www.uniprot.org/uniprot/DNPH1_RAT DNPH1_RAT] Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.<ref>PMID:17234634</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Buffalo rat]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Kaminski, P A]] | + | [[Category: Rattus norvegicus]] |
- | [[Category: Labesse, G]] | + | [[Category: Kaminski PA]] |
- | [[Category: Padilla, A]] | + | [[Category: Labesse G]] |
- | [[Category: Yang, Y]] | + | [[Category: Padilla A]] |
- | [[Category: Zhang, C]] | + | [[Category: Yang Y]] |
- | [[Category: Gmp]]
| + | [[Category: Zhang C]] |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: N-glycosidase]]
| + | |
- | [[Category: Nucleus]]
| + | |
- | [[Category: Phosphoprotein]]
| + | |
- | [[Category: Protein]]
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| Structural highlights
Function
DNPH1_RAT Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The gene Rcl encodes a deoxynucleoside 5'-monophosphate N-glycosidase that catalyzes the hydrolysis of the N-glycosidic bond of the nucleotide to give deoxyribose 5-phosphate and a nucleobase, preferentially a purine. This enzyme is over-expressed in several cancers, and its rate of expression is correlated to the degree of aggressiveness of tumors, which makes it a new and attractive therapeutic target. We describe here its structural characterization in the presence of two inhibitory substrate mimics. One of these ligands corresponds to the monophosphorylated form of acyclovir, which is used in the clinic. This study reveals an important ligand-induced stabilization of the dimer structure of the enzyme. The original structural features of Rcl will be helpful for designing new inhibitors.
Structural characterization of the mammalian deoxynucleotide N-hydrolase Rcl and its stabilizing interactions with two inhibitors.,Yang Y, Padilla A, Zhang C, Labesse G, Kaminski PA J Mol Biol. 2009 Dec 4;394(3):435-47. Epub 2009 Oct 12. PMID:19822152[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghiorghi YK, Zeller KI, Dang CV, Kaminski PA. The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5'-monophosphate N-glycosidase. J Biol Chem. 2007 Mar 16;282(11):8150-6. Epub 2007 Jan 18. PMID:17234634 doi:http://dx.doi.org/10.1074/jbc.M610648200
- ↑ Yang Y, Padilla A, Zhang C, Labesse G, Kaminski PA. Structural characterization of the mammalian deoxynucleotide N-hydrolase Rcl and its stabilizing interactions with two inhibitors. J Mol Biol. 2009 Dec 4;394(3):435-47. Epub 2009 Oct 12. PMID:19822152 doi:http://dx.doi.org/10.1016/j.jmb.2009.10.004
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