8d6l

Q108K:K40L:T51C:T53A:R58L:Q38F:Q4F mutant of hCRBPII bound to synthetic fluorophore CM1V

spinqualitylabelsall models 8d6l, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8d6l is a 1 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 1.69Å Ligands: GOL, RH6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RET2_HUMAN Intracellular transport of retinol. Publication Abstract from PubMed Cysteine-based Michael addition is a widely employed strategy for covalent conjugation of proteins, peptides, and drugs. The covalent reaction is irreversible in most cases, leading to a lack of control over the process. Utilizing spectroscopic analyses along with X-ray crystallographic studies, we demonstrate Michael addition of an engineered cysteine residue in human Cellular Retinol Binding Protein II (hCRBPII) with a coumarin analog that creates a non-fluorescent complex. UV-illumination reverses the conjugation, yielding a fluorescent species, presumably through a retro-Michael process. This series of events can be repeated between a bound and non-bound form of the cysteine reversibly, resulting in the ON-OFF control of fluorescence. The details of the mechanism of photoswitching was illuminated by recapitulation of the process in light irradiated single crystals, confirming the mechanism at atomic resolution. Light controlled reversible Michael addition of cysteine: a new tool for dynamic site-specific labeling of proteins.,Maity S, Bingham C, Sheng W, Ehyaei N, Chakraborty D, Tahmasebi-Nick S, Kimmel TE, Vasileiou C, Geiger JH, Borhan B Analyst. 2023 Feb 27;148(5):1085-1092. doi: 10.1039/d2an01395a. PMID:36722993 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Retinol-binding protein 3D structures

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