4QGV

Crystal structure of the R132K:R111L mutant of Cellular Retinoic Acid Binding ProteinII complexed with a synthetic ligand (Merocyanine) at 1.73 angstrom resolution.

4QGV の概要

• エントリーDOI: 10.2210/pdb4qgv/pdb
• 関連するPDBエントリー: 2G7B 3F8A 3FEP 4EEJ 4EXZ 4I9S 4QGW 4QGX
• 分子名称: Cellular 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 (3 entities in total)
• 機能のキーワード: protein engineering, protein fluorescence merocyanine dyes for fluorescent protein labeling, fluorescent protein tag, merocyanine protonated schiff base, iminium, protein binding
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31286.87

構造登録者

Nosrati, M.,Yapici, I.,Geiger, J.H. (登録日: 2014-05-25, 公開日: 2015-01-28, 最終更新日: 2024-11-27)

主引用文献

Yapici, 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

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

実験手法

X-RAY DIFFRACTION (1.73 Å)