4u8h: Difference between revisions
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==Crystal Structure of Mammalian Period-Cryptochrome Complex== | ==Crystal Structure of Mammalian Period-Cryptochrome Complex== | ||
<StructureSection load='4u8h' size='340' side='right' caption='[[4u8h]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4u8h' size='340' side='right' caption='[[4u8h]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
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<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> | <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 id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[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> | <tr id='resources'><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://pdbe.org/4u8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u8h RCSB], [http://www.ebi.ac.uk/pdbsum/4u8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u8h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4u8h" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:10, 4 August 2016
Crystal Structure of Mammalian Period-Cryptochrome ComplexCrystal Structure of Mammalian Period-Cryptochrome Complex
Structural highlights
Function[PER2_MOUSE] Component of the circadian clock mechanism which is essential for generating circadian rhythms. Negative element in the circadian transcriptional loop. Influences clock function by interacting with other circadian regulatory proteins and transporting them to the nucleus. Negatively regulates CLOCK|NPAS2-BMAL1|BMAL2-induced transactivation.[1] [2] Publication 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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