4i9s | pdb_00004i9s

Crystal Structure of the R111K:R132L:Y134F:T54V:R59W Mutant of the Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans Retinal at 2.58 Angstrom Resolution

spinqualitylabelsall models 4i9s, resolution 2.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i9s 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 2.58Å Ligands: RET 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 Reengineering of Cellular Retinoic Acid Binding Protein II (CRABPII) to be capable of binding retinal as a protonated Schiff base is described. Through rational alterations of the binding pocket, electrostatic perturbations of the embedded retinylidene chromophore that favor charge delocalization of the iminium charge lead to exquisite control in the regulation of chromophoric absorption properties, spanning the visible spectrum (474-640 nm). The pKa of the retinylidine protonated Schiff base was modulated from 2.4 to 8.1, giving rise to a set of proteins of varying colors and pH sensitivities. These proteins were used to demonstrate a concentration independent, ratiometric pH sensor. Rational Design of a Colorimetric pH Sensor from a Soluble Retinoic Acid Chaperone.,Berbasova T, Nosrati M, Vasileiou C, Wang W, Lee KS, Yapici I, Geiger JH, Borhan B J Am Chem Soc. 2013 Sep 20. PMID:24059243 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cellular retinoic acid-binding protein 3D structures Gustavo Elberto Epalza Sanchez/Sandbox 1

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