View source for 8vzz


==Q108K:K40L:T51V:T53S:Y19W:R58W mutant of hCRBPII bound to synthetic fluorophore TD-1V==
<StructureSection load='8vzz' size='340' side='right'caption='[[8vzz]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8vzz]] 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=8VZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VZZ 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]] 1.22&#8491;</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=8vzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vzz OCA], [https://pdbe.org/8vzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vzz RCSB], [https://www.ebi.ac.uk/pdbsum/8vzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vzz 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8vzz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bingham CR]]
[[Category: Borhan B]]
[[Category: Geiger JH]]
[[Category: Nosssoni Z]]