View source for 6lhu


==High resolution structure of FANCA C-terminal domain (CTD)==
<StructureSection load='6lhu' size='340' side='right'caption='[[6lhu]], [[Resolution|resolution]] 3.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lhu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LHU 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]] 3.46&#8491;</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=6lhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lhu OCA], [https://pdbe.org/6lhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lhu RCSB], [https://www.ebi.ac.uk/pdbsum/6lhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lhu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q4VT51_XENLA Q4VT51_XENLA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Monoubiquitination of the Fanconi anemia complementation group D2 (FANCD2) protein by the FA core ubiquitin ligase complex is the central event in the FA pathway. FANCA and FANCG play major roles in the nuclear localization of the FA core complex. Mutations of these two genes are the most frequently observed genetic alterations in FA patients, and most point mutations in FANCA are clustered in the C-terminal domain (CTD). To understand the basis of the FA-associated FANCA mutations, we determined the cryo-electron microscopy (EM) structures of Xenopus laevis FANCA alone at 3.35 A and 3.46 A resolution and two distinct FANCA-FANCG complexes at 4.59 and 4.84 A resolution, respectively. The FANCA CTD adopts an arc-shaped solenoid structure that forms a pseudo-symmetric dimer through its outer surface. FA- and cancer-associated point mutations are widely distributed over the CTD. The two different complex structures capture independent interactions of FANCG with either FANCA C-terminal HEAT repeats, or the N-terminal region. We show that mutations that disturb either of these two interactions prevent the nuclear localization of FANCA, thereby leading to an FA pathway defect. The structure provides insights into the function of FANCA CTD, and provides a framework for understanding FA- and cancer-associated mutations.

Structural basis of the fanconi anemia-associated mutations within the FANCA and FANCG complex.,Jeong E, Lee SG, Kim HS, Yang J, Shin J, Kim Y, Kim J, Scharer OD, Kim Y, Yeo JE, Kim HM, Cho Y Nucleic Acids Res. 2020 Jan 31. pii: 5718259. doi: 10.1093/nar/gkaa062. PMID:32002546<ref>PMID:32002546</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lhu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Cho Y]]
[[Category: Jeong E]]
[[Category: Kim H]]
[[Category: Kim J]]
[[Category: Kim Y]]
[[Category: Lee S]]
[[Category: Scharer O]]
[[Category: Shin J]]