9pn1

Crystal structure of Q108K:K40L:T51V:T53C:R58W:T29L:Y19W:Q4A mutant of cellular retinol binding protein II complex with 15-cis-retinal

spinqualitylabelsall models 9pn1, resolution 1.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9pn1 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.26Å Ligands: ACT, GOL, RET Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RET2_HUMAN Intracellular transport of retinol. Publication Abstract from PubMed We describe the photoisomerization of the retinylidene protonated Schiff base in human retinol-binding protein II (hCRBPII) and the role of water molecules in this process. We characterize the photoisomerization of the 15-cis/all-trans retinylidene protonated Schiff base in this system using UV-visible spectroscopy and atomic-resolution X-ray crystallography. We further demonstrate a process where the pK(a) of the protonated Schiff base is substantially altered by light-induced dehydration of the binding pocket, suggesting novel pathways of photoswitching that rely not on isomerization or conformational change of the chromophore but rather on light-induced reorganization of the protein environment. Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system.,Ehyaei N, Bingham C, Silva K, Nossoni Z, Gavgani HN, Nosrati M, Eaves J, Akhdar M, Vasileiou C, Borhan B, Geiger JH Acta Crystallogr D Struct Biol. 2026 Jun 1;82(Pt 6):664-671. doi: , 10.1107/S2059798326003839. Epub 2026 May 27. PMID:42201784 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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