4u8h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4u8h]] is a 4 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=4U8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U8H FirstGlance]. <br> | <table><tr><td colspan='2'>[[4u8h]] is a 4 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=4U8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U8H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.798Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4u8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u8h OCA], [https://pdbe.org/4u8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u8h RCSB], [https://www.ebi.ac.uk/pdbsum/4u8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u8h 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=4u8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u8h OCA], [https://pdbe.org/4u8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u8h RCSB], [https://www.ebi.ac.uk/pdbsum/4u8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u8h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 10:26, 27 September 2023
Crystal Structure of Mammalian Period-Cryptochrome ComplexCrystal Structure of Mammalian Period-Cryptochrome Complex
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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