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New page: left|200px<br /> <applet load="1mq0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mq0, resolution 2.40Å" /> '''Crystal Structure o...
 
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[[Image:1mq0.gif|left|200px]]<br />
<applet load="1mq0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mq0, resolution 2.40&Aring;" />
'''Crystal Structure of Human Cytidine Deaminase'''<br />


==Overview==
==Crystal Structure of Human Cytidine Deaminase==
Human cytidine deaminase (CDA) is an enzyme prominent for its role in, catalyzing metabolic processing of nucleoside-type anticancer and, antiviral agents. It is thus a promising target for the development of, small molecule therapeutic adjuvants. We report the first crystal, structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to, establish a canonical pi/pi-interaction with a key active site residue, Phe 137.
<StructureSection load='1mq0' size='340' side='right'caption='[[1mq0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mq0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQ0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRD:1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE'>BRD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1mq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq0 OCA], [https://pdbe.org/1mq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mq0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mq0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDD_HUMAN CDD_HUMAN] This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mq/1mq0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mq0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical pi/pi-interaction with a key active site residue, Phe 137.


==Disease==
Structure of human cytidine deaminase bound to a potent inhibitor.,Chung SJ, Fromme JC, Verdine GL J Med Chem. 2005 Feb 10;48(3):658-60. PMID:15689149<ref>PMID:15689149</ref>
Known disease associated with this structure: Anemia, congenital dyserythropoietic, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607465 607465]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1MQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and BRD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytidine_deaminase Cytidine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.5 3.5.4.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MQ0 OCA].
</div>
<div class="pdbe-citations 1mq0" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of human cytidine deaminase bound to a potent inhibitor., Chung SJ, Fromme JC, Verdine GL, J Med Chem. 2005 Feb 10;48(3):658-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15689149 15689149]
*[[Deaminase 3D structures|Deaminase 3D structures]]
[[Category: Cytidine deaminase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chung, S.J.]]
[[Category: Chung SJ]]
[[Category: Fromme, J.C.]]
[[Category: Fromme JC]]
[[Category: Verdine, G.L.]]
[[Category: Verdine GL]]
[[Category: BRD]]
[[Category: ZN]]
[[Category: amine hydrolase]]
[[Category: anticancer]]
[[Category: chemotherapy]]
[[Category: cytidine deaminase]]
[[Category: diazepinone]]
[[Category: drug]]
[[Category: edge-to-face interaction]]
[[Category: enzyme]]
[[Category: human]]
[[Category: inhibitor]]
[[Category: leukemia]]
[[Category: phi-phi interaction]]
[[Category: protein]]
[[Category: zinc]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:13:44 2007''

Latest revision as of 06:07, 1 October 2025

Crystal Structure of Human Cytidine Deaminase

1mq0, resolution 2.40Å

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