3c5r

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{{Seed}}
 
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[[Image:3c5r.png|left|200px]]
 
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==Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences==
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The line below this paragraph, containing "STRUCTURE_3c5r", creates the "Structure Box" on the page.
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<StructureSection load='3c5r' size='340' side='right'caption='[[3c5r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_3c5r| PDB=3c5r | SCENE= }}
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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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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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The line below this paragraph, {{ABSTRACT_PUBMED_18480049}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3c5r" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18480049 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18480049}}
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Breast cancer, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601593 601593]]
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==About this Structure==
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3C5R is a [[Single protein]] structure of 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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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18480049 18480049]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: III, D Fox.]]
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[[Category: Fox III D]]
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[[Category: Klevit, R E.]]
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[[Category: Klevit RE]]
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[[Category: Stenkamp, R E.]]
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[[Category: Le Trong I]]
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[[Category: Trong, I Le.]]
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[[Category: Stenkamp RE]]
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[[Category: Ank repeat]]
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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: Polymorphism]]
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[[Category: Protein]]
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[[Category: Protein binding]]
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[[Category: Ubl conjugation]]
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[[Category: Zinc]]
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[[Category: Zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 6 09:54:24 2008''
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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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