5dju: Difference between revisions
New page: '''Unreleased structure''' The entry 5dju is ON HOLD until Paper Publication Authors: Tarnawski, M., Wang, H., Yumerefendi, H., Hahn, K.M., Schlichting, I. Description: [[Category: Un... |
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==Crystal structure of LOV2 (C450A) domain in complex with Zdk3== | |||
<StructureSection load='5dju' size='340' side='right'caption='[[5dju]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dju]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Avena_sativa Avena sativa] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DJU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=5dju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dju OCA], [https://pdbe.org/5dju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dju RCSB], [https://www.ebi.ac.uk/pdbsum/5dju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dju ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O49004_AVESA O49004_AVESA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
LOVTRAP is an optogenetic approach for reversible light-induced protein dissociation using protein A fragments that bind to the LOV domain only in the dark, with tunable kinetics and a >150-fold change in the dissociation constant (Kd). By reversibly sequestering proteins at mitochondria, we precisely modulated the proteins' access to the cell edge, demonstrating a naturally occurring 3-mHz cell-edge oscillation driven by interactions of Vav2, Rac1, and PI3K proteins. | |||
LOVTRAP: an optogenetic system for photoinduced protein dissociation.,Wang H, Vilela M, Winkler A, Tarnawski M, Schlichting I, Yumerefendi H, Kuhlman B, Liu R, Danuser G, Hahn KM Nat Methods. 2016 Jul 18. doi: 10.1038/nmeth.3926. PMID:27427858<ref>PMID:27427858</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5dju" style="background-color:#fffaf0;"></div> | ||
[[Category: Hahn | == References == | ||
[[Category: Tarnawski | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Avena sativa]] | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | |||
[[Category: Hahn KM]] | |||
[[Category: Schlichting I]] | |||
[[Category: Tarnawski M]] | |||
[[Category: Wang H]] | |||
[[Category: Yumerefendi H]] |
Latest revision as of 00:44, 29 June 2023
Crystal structure of LOV2 (C450A) domain in complex with Zdk3Crystal structure of LOV2 (C450A) domain in complex with Zdk3
Structural highlights
FunctionPublication Abstract from PubMedLOVTRAP is an optogenetic approach for reversible light-induced protein dissociation using protein A fragments that bind to the LOV domain only in the dark, with tunable kinetics and a >150-fold change in the dissociation constant (Kd). By reversibly sequestering proteins at mitochondria, we precisely modulated the proteins' access to the cell edge, demonstrating a naturally occurring 3-mHz cell-edge oscillation driven by interactions of Vav2, Rac1, and PI3K proteins. LOVTRAP: an optogenetic system for photoinduced protein dissociation.,Wang H, Vilela M, Winkler A, Tarnawski M, Schlichting I, Yumerefendi H, Kuhlman B, Liu R, Danuser G, Hahn KM Nat Methods. 2016 Jul 18. doi: 10.1038/nmeth.3926. PMID:27427858[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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