4u8h: Difference between revisions
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''' | ==Crystal Structure of Mammalian Period-Cryptochrome Complex== | ||
<StructureSection load='4u8h' size='340' side='right' caption='[[4u8h]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4u8h]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U8H FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u8h RCSB], [http://www.ebi.ac.uk/pdbsum/4u8h PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mammalian circadian clock is driven by a transcriptional-translational feedback loop, which produces robust 24-hr rhythms. Proper oscillation of the clock depends on the complex formation and periodic turnover of the Period and Cryptochrome proteins, which together inhibit their own transcriptional activator complex, CLOCK-BMAL1. We determined the crystal structure of the CRY-binding domain (CBD) of PER2 in complex with CRY2 at 2.8 A resolution. PER2-CBD adopts a highly extended conformation, embracing CRY2 with a sinuous binding mode. Its N-terminal end tucks into CRY adjacent to a large pocket critical for CLOCK-BMAL1 binding, while its C-terminal half flanks the CRY2 C-terminal helix and sterically hinders the recognition of CRY2 by the FBXL3 ubiquitin ligase. Unexpectedly, a strictly conserved intermolecular zinc finger, whose integrity is important for clock rhythmicity, further stabilizes the complex. Our structure-guided analyses show that these interspersed CRY-interacting regions represent multiple functional modules of PERs at the CRY-binding interface.DOI: http://dx.doi.org/10.7554/eLife.03674.001. | |||
Molecular assembly of the period-cryptochrome circadian transcriptional repressor complex.,Nangle SN, Rosensweig C, Koike N, Tei H, Takahashi JS, Green CB, Zheng N Elife. 2014 Aug 15;3:e03674. doi: 10.7554/eLife.03674. PMID:25127877<ref>PMID:25127877</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Green, C B.]] | |||
[[Category: Koike, N.]] | |||
[[Category: Nangle, S N.]] | |||
[[Category: Rosensweig, C.]] | |||
[[Category: Takahashi, J S.]] | |||
[[Category: Tei, H.]] | |||
[[Category: Zheng, N.]] | |||
[[Category: Circadian clock protein-transcription complex]] | |||
[[Category: Transcriptional repression]] | |||
[[Category: Zinc-binding]] |