3c5r

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[[Image:3c5r.png|left|200px]]
 
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{{STRUCTURE_3c5r| PDB=3c5r | SCENE= }}
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==Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences==
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<StructureSection load='3c5r' size='340' side='right'caption='[[3c5r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3c5r]] 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=3C5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C5R FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5r OCA], [https://pdbe.org/3c5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c5r RCSB], [https://www.ebi.ac.uk/pdbsum/3c5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c5r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BARD1_HUMAN BARD1_HUMAN] Probable E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.<ref>PMID:10477523</ref> <ref>PMID:12890688</ref> <ref>PMID:14976165</ref> <ref>PMID:20351172</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c5/3c5r_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3c5r ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BARD1 is the constitutive nuclear partner to the breast and ovarian cancer-specific tumor suppressor BRCA1. Together, they form a heterodimeric complex responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. We report the 2.0A structure of the BARD1 ankyrin repeat domain. The structure includes four ankyrin repeats with a non-canonical C-terminal capping ankyrin repeat and a well ordered extended loop preceding the first repeat. Conserved surface features show an acidic patch and an acidic pocket along the surface typically used by ankyrin repeat domains for binding cognate proteins. We also demonstrate that two reported mutations, N470S and V507M, in the ankyrin repeat domain do not result in observable structural defects. These results provide a structural basis for exploring the biological function of the ankyrin repeat domain and for modeling BARD1 isoforms.
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===Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences===
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Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences.,Fox D 3rd, Le Trong I, Rajagopal P, Brzovic PS, Stenkamp RE, Klevit RE J Biol Chem. 2008 Jul 25;283(30):21179-86. Epub 2008 May 14. PMID:18480049<ref>PMID:18480049</ref>
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{{ABSTRACT_PUBMED_18480049}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 3c5r" style="background-color:#fffaf0;"></div>
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[[3c5r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C5R OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:018480049</ref><references group="xtra"/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: III, D Fox.]]
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[[Category: Large Structures]]
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[[Category: Klevit, R E.]]
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[[Category: Fox III D]]
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[[Category: Stenkamp, R E.]]
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[[Category: Klevit RE]]
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[[Category: Trong, I Le.]]
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[[Category: Le Trong I]]
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[[Category: Ank repeat]]
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[[Category: Stenkamp RE]]
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[[Category: Ankyrin repeat]]
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[[Category: Bard1]]
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[[Category: Disease mutation]]
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[[Category: Extended loop]]
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[[Category: Four repeat]]
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[[Category: Helix]]
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[[Category: Metal-binding]]
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[[Category: Nucleus]]
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[[Category: Protein]]
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[[Category: Protein binding]]
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[[Category: Zinc-finger]]
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Current revision

Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences

PDB ID 3c5r

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