4i6g: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4i6g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I6G FirstGlance]. <br>
<table><tr><td colspan='2'>[[4i6g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I6G FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4i6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i6g OCA], [https://pdbe.org/4i6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i6g RCSB], [https://www.ebi.ac.uk/pdbsum/4i6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i6g 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=4i6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i6g OCA], [https://pdbe.org/4i6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i6g RCSB], [https://www.ebi.ac.uk/pdbsum/4i6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i6g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/CRY2_MOUSE CRY2_MOUSE]  
[https://www.uniprot.org/uniprot/CRY2_MOUSE CRY2_MOUSE]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cryptochrome (CRY) flavoproteins act as blue-light receptors in plants and insects, but perform light-independent functions at the core of the mammalian circadian clock. To drive clock oscillations, mammalian CRYs associate with the Period proteins (PERs) and together inhibit the transcription of their own genes. The SCF(FBXL3) ubiquitin ligase complex controls this negative feedback loop by promoting CRY ubiquitination and degradation. However, the molecular mechanisms of their interactions and the functional role of flavin adenine dinucleotide (FAD) binding in CRYs remain poorly understood. Here we report crystal structures of mammalian CRY2 in its apo, FAD-bound and FBXL3-SKP1-complexed forms. Distinct from other cryptochromes of known structures, mammalian CRY2 binds FAD dynamically with an open cofactor pocket. Notably, the F-box protein FBXL3 captures CRY2 by simultaneously occupying its FAD-binding pocket with a conserved carboxy-terminal tail and burying its PER-binding interface. This novel F-box-protein-substrate bipartite interaction is susceptible to disruption by both FAD and PERs, suggesting a new avenue for pharmacological targeting of the complex and a multifaceted regulatory mechanism of CRY ubiquitination.
SCFFBXL3 ubiquitin ligase targets cryptochromes at their cofactor pocket.,Xing W, Busino L, Hinds TR, Marionni ST, Saifee NH, Bush MF, Pagano M, Zheng N Nature. 2013 Apr 4;496(7443):64-8. doi: 10.1038/nature11964. Epub 2013 Mar 17. PMID:23503662<ref>PMID:23503662</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4i6g" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cryptochrome|Cryptochrome]]
*[[Cryptochrome|Cryptochrome]]
*[[Cryptochrome 3D structures|Cryptochrome 3D structures]]
*[[Cryptochrome 3D structures|Cryptochrome 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 11:50, 1 March 2024

a vertebrate cryptochrome with FAD

4i6g, resolution 2.20Å

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