3fep
Crystal structure of the R132K:R111L:L121E:R59W-CRABPII mutant complexed with a synthetic ligand (merocyanin) at 2.60 angstrom resolution.Crystal structure of the R132K:R111L:L121E:R59W-CRABPII mutant complexed with a synthetic ligand (merocyanin) at 2.60 angstrom resolution.
Structural highlights
FunctionRABP2_HUMAN Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
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