View source for 9frx


==Porcine Retinol-Binding Protein 3 (RBP3)==
<StructureSection load='9frx' size='340' side='right'caption='[[9frx]], [[Resolution|resolution]] 3.67&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9frx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FRX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.67&#8491;</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=9frx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9frx OCA], [https://pdbe.org/9frx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9frx RCSB], [https://www.ebi.ac.uk/pdbsum/9frx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9frx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A287A908_PIG A0A287A908_PIG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The vertebrate visual cycle hinges on enzymatically converting all-trans-retinol (at-ROL) into 11-cis-retinal (11c-RAL), the chromophore that binds to opsins in photoreceptors, forming light-responsive pigments. When struck by a photon, these pigments activate the phototransduction pathway and initiate the process of vision. The enzymatic isomerization of at-ROL, crucial for restoring the visual pigments and preparing them to receive new light stimuli, relies on various enzymes found in both the photoreceptors and retinal pigment epithelium cells. To function effectively, retinoids must shuttle between these two cell types. Retinol-binding protein 3 (RBP3), located in the interphotoreceptor matrix, probably plays a pivotal role in this transport mechanism. Comprised of four retinoid-binding modules, RBP3 also binds fatty acids, potentially aiding retinal function by facilitating the loading and unloading of different retinoids at specific cell types thereby directing the cycle. In this study, we present a 3.67 A cryoEM structure of porcine RBP3, along with molecular docking analysis and corroborative in-solution small-angle X-ray scattering data for titration of RBP3 with relevant ligands, that also give insights on RBP3 conformational adaptability.

CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3.,Kaushik V, Gessa L, Kumar N, Pinkas M, Czarnocki-Cieciura M, Palczewski K, Novacek J, Fernandes H Open Biol. 2025 Jan;15(1):240180. doi: 10.1098/rsob.240180. Epub 2025 Jan 22. PMID:39837501<ref>PMID:39837501</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9frx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Czarnocki-Cieciura M]]
[[Category: Fernandes H]]
[[Category: Gessa L]]
[[Category: Kaushik V]]
[[Category: Kumar N]]
[[Category: Novacek J]]
[[Category: Palczewski K]]
[[Category: Pinkas M]]