A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4
Tekijät: Repo S, Paidanius TA, Hytonen VP, Nyholm TKM, Hailing KK, Huuskonen J, Pentikainen T, Rissanen K, Slotte JP, Airenne TT, Salminen TA, Kulomaa MS, Johnson MS
Kustantaja: CELL PRESS
Julkaisuvuosi: 2006
Journal: Chemistry and Biology
Tietokannassa oleva lehden nimi: CHEMISTRY & BIOLOGY
Lehden akronyymi: CHEM BIOL
Vuosikerta: 13
Numero: 10
Aloitussivu: 1029
Lopetussivu: 1039
Sivujen määrä: 11
ISSN: 1074-5521
DOI: https://doi.org/10.1016/j.chembiol.2006.08.006
Tiivistelmä
The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands beta 3 and beta 4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 angstrom) X-ray structure for avidin reported here. These results may be valuable in designing improved tools for avidin-based life science and nanobiotechnology applications.
The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands beta 3 and beta 4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 angstrom) X-ray structure for avidin reported here. These results may be valuable in designing improved tools for avidin-based life science and nanobiotechnology applications.
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