9frx

Porcine Retinol-Binding Protein 3 (RBP3)

spinqualitylabelsall models 9frx, resolution 3.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9frx is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.67Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A287A908_PIG 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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