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4QGW

Crystal sturcture of the R132K:R111L:L121D mutant of Cellular Retinoic Acid Binding ProteinII complexed with a synthetic ligand (Merocyanine) at 1.77 angstrom resolution

Summary for 4QGW
Entry DOI10.2210/pdb4qgw/pdb
Related2G7B 3F8A 3FEP 4EEJ 4EXZ 4I9R 4QGV 4QGX
DescriptorCellular retinoic acid-binding protein 2, (2E,4E,6E)-3-methyl-6-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)hexa-2,4-dienal, 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
Functional Keywordsprotein engineering, protein fluorescence, merocyanine dyes for fluorescent protein labeling, fluorescent protein tag, merocyanine protonated schiff base iminium, protein binding
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P29373
Total number of polymer chains2
Total formula weight31573.07
Authors
Nosrati, M.,Yapici, I.,Geiger, J.H. (deposition date: 2014-05-26, release date: 2015-01-28, Last modification date: 2015-02-11)
Primary citationYapici, I.,Lee, K.S.,Berbasova, T.,Nosrati, M.,Jia, X.,Vasileiou, C.,Wang, W.,Santos, E.M.,Geiger, J.H.,Borhan, B.
"Turn-on" protein fluorescence: in situ formation of cyanine dyes.
J.Am.Chem.Soc., 137:1073-1080, 2015
Cited by
PubMed Abstract: 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.
PubMed: 25534273
DOI: 10.1021/ja506376j
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.77 Å)
Structure validation

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