6tni
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of FANCD2 homodimer== | |
+ | <SX load='6tni' size='340' side='right' viewer='molstar' caption='[[6tni]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6tni]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TNI FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=6tni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tni OCA], [https://pdbe.org/6tni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tni RCSB], [https://www.ebi.ac.uk/pdbsum/6tni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tni ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/F1NP22_CHICK F1NP22_CHICK] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Vertebrate DNA crosslink repair excises toxic replication-blocking DNA crosslinks. Numerous factors involved in crosslink repair have been identified, and mutations in their corresponding genes cause Fanconi anemia (FA). A key step in crosslink repair is monoubiquitination of the FANCD2-FANCI heterodimer, which then recruits nucleases to remove the DNA lesion. Here, we use cryo-EM to determine the structures of recombinant chicken FANCD2 and FANCI complexes. FANCD2-FANCI adopts a closed conformation when the FANCD2 subunit is monoubiquitinated, creating a channel that encloses double-stranded DNA (dsDNA). Ubiquitin is positioned at the interface of FANCD2 and FANCI, where it acts as a covalent molecular pin to trap the complex on DNA. In contrast, isolated FANCD2 is a homodimer that is unable to bind DNA, suggestive of an autoinhibitory mechanism that prevents premature activation. Together, our work suggests that FANCD2-FANCI is a clamp that is locked onto DNA by ubiquitin, with distinct interfaces that may recruit other DNA repair factors. | ||
- | + | FANCD2-FANCI is a clamp stabilized on DNA by monoubiquitination of FANCD2 during DNA repair.,Alcon P, Shakeel S, Chen ZA, Rappsilber J, Patel KJ, Passmore LA Nat Struct Mol Biol. 2020 Feb 17. pii: 10.1038/s41594-020-0380-1. doi:, 10.1038/s41594-020-0380-1. PMID:32066963<ref>PMID:32066963</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6tni" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </SX> | ||
+ | [[Category: Gallus gallus]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Alcon P]] | ||
+ | [[Category: Passmore LA]] | ||
+ | [[Category: Shakeel S]] |
Current revision
Structure of FANCD2 homodimer
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