8w00: Difference between revisions
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The | ==Q108K:K40L:T51V:T53S:Y19W:R58W:L117E mutant of hCRBPII bound to synthetic fluorophore TD-1V== | ||
<StructureSection load='8w00' size='340' side='right'caption='[[8w00]], [[Resolution|resolution]] 1.23Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8w00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8W00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8W00 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]] 1.23Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1AEQ:(2E)-3-{5-[4-(dimethylamino)phenyl]thiophen-2-yl}but-2-enal'>A1AEQ</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=8w00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8w00 OCA], [https://pdbe.org/8w00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8w00 RCSB], [https://www.ebi.ac.uk/pdbsum/8w00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8w00 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN] Intracellular transport of retinol. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human cellular retinol binding protein II (hCRBPII) was used as a protein engineering platform to rationally regulate absorptive and emissive properties of a covalently bound fluorogenic dye. We demonstrate the binding of a thio-dapoxyl analog via formation of a protonated imine between an active site lysine residue and the chromophore's aldehyde. Rational manipulation of the electrostatics of the binding pocket results in a 204 nm shift in absorption and a 131 nm shift in emission. The protein is readily expressed in mammalian systems and binds with exogenously delivered fluorophore as demonstrated by live-cell imaging experiments. | |||
Regulation of Absorption and Emission in a Protein/Fluorophore Complex.,Santos EM, Chandra I, Assar Z, Sheng W, Ghanbarpour A, Bingham C, Vasileiou C, Geiger JH, Borhan B ACS Chem Biol. 2024 Jul 24. doi: 10.1021/acschembio.4c00125. PMID:39046136<ref>PMID:39046136</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8w00" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bingham CR]] | |||
[[Category: Geiger JH]] | |||
[[Category: Nossoni Z]] | |||
Latest revision as of 05:53, 7 August 2024
Q108K:K40L:T51V:T53S:Y19W:R58W:L117E mutant of hCRBPII bound to synthetic fluorophore TD-1V
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