View source for 7lsq


==The Crystal Structure of Q108K:K40E:T53A:R58W:Q38F:Q4F:Y19W Mutant of HCRBPII Bound with LizFluor Chromophore Showing Excited State Intermolecular Proton Transfer==
<StructureSection load='7lsq' size='340' side='right'caption='[[7lsq]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7lsq]] is a 4 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=7LSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LSQ 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]] 1.6713054&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZFG:4-{5-[(2E)-but-2-en-2-yl]thiophen-2-yl}-N,N-dimethylaniline'>ZFG</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=7lsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lsq OCA], [https://pdbe.org/7lsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lsq RCSB], [https://www.ebi.ac.uk/pdbsum/7lsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lsq 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 ==
The incredible potential for fluorescent proteins to revolutionize biology has inspired the development of a variety of design strategies to address an equally broad range of photophysical characteristics, depending on potential applications. Of these, fluorescent proteins that simultaneously exhibit high quantum yield, red-shifted emission, and wide separation between excitation and emission wavelengths (Large Stokes Shift, LSS) are rare. The pursuit of LSS systems has led to the formation of a complex, obtained from the marriage of a rationally engineered protein (human cellular retinol binding protein II, hCRBPII) and different fluorogenic molecules, capable of supporting photobase activity. The large increase in basicity upon photoexcitation leads to protonation of the fluorophore in the excited state, dramatically red-shifting its emission, leading to an LSS protein/fluorophore complex. Essential for selective photobase activity is the intimate involvement of the target protein structure and sequence that enables Excited State Proton Transfer (ESPT). The potential power and usefulness of the strategy was demonstrated in live cell imaging of human cell lines.

Design of Large Stokes Shift Fluorescent Proteins Based on Excited State Proton Transfer of an Engineered Photobase.,Santos EM, Sheng W, Esmatpour Salmani R, Tahmasebi Nick S, Ghanbarpour A, Gholami H, Vasileiou C, Geiger JH, Borhan B J Am Chem Soc. 2021 Sep 22;143(37):15091-15102. doi: 10.1021/jacs.1c05039. Epub, 2021 Sep 13. PMID:34516091<ref>PMID:34516091</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lsq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Geiger J]]
[[Category: Ghanbarpour A]]