4qgx

Crystal structure of the R132K:R111L:L121E mutant of Cellular Retinoic Acid Binding ProteinII complexed with a synthetic ligand (Merocyanine) at 1.47 angstrom resolution

spinqualitylabelsall models 4qgx, resolution 1.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qgx 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 1.471Å Ligands: LMC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RABP2_HUMAN Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. Publication Abstract from PubMed Protein reengineering of cellular retinoic acid binding protein II (CRABPII) has yielded a genetically addressable system, capable of binding a profluorophoric chromophore that results in fluorescent protein/chromophore complexes. These complexes exhibit far-red emission, with high quantum efficiencies and brightness and also exhibit excellent pH stability spanning the range of 2-11. In the course of this study, it became evident that single mutations of L121E and R59W were most effective in improving the fluorescent characteristics of CRABPII mutants as well as the kinetics of complex formation. The readily crystallizable nature of these proteins was invaluable to provide clues for the observed spectroscopic behavior that results from single mutation of key residues. "Turn-On" Protein Fluorescence: In Situ Formation of Cyanine Dyes.,Yapici I, Lee KS, Berbasova T, Nosrati M, Jia X, Vasileiou C, Wang W, Santos EM, Geiger JH, Borhan B J Am Chem Soc. 2015 Jan 14. PMID:25534273 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cellular retinoic acid-binding protein 3D structures

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