3fa2

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<StructureSection load='3fa2' size='340' side='right'caption='[[3fa2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3fa2' size='340' side='right'caption='[[3fa2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3fa2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FA2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3fa2]] 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=3FA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FA2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BARD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3fa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fa2 OCA], [https://pdbe.org/3fa2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fa2 RCSB], [https://www.ebi.ac.uk/pdbsum/3fa2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fa2 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=3fa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fa2 OCA], [https://pdbe.org/3fa2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fa2 RCSB], [https://www.ebi.ac.uk/pdbsum/3fa2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fa2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[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>
== 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>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[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: Bard1]]
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[[Category: Brca1]]
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[[Category: Brca1 c-terminal domain]]
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[[Category: Brct]]
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[[Category: Disease mutation]]
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[[Category: Metal-binding]]
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[[Category: Nucleus]]
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[[Category: Protein binding]]
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[[Category: Tandem]]
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[[Category: Zinc-finger]]
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Revision as of 06:43, 6 September 2023

Crystal Structure of the BRCA1 Associated Ring Domain (BARD1) Tandem BRCT Domains

PDB ID 3fa2

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