Binding Properties of HABA-Type Azo Derivatives to Avidin and Avidin-Related Protein 4
| Autor: | J. Peter Slotte, Thomas K.M. Nyholm, Juhani Huuskonen, Kari Rissanen, Tiina Paldanius, Tiina A. Salminen, Tomi T. Airenne, Katrin K. Halling, Vesa P. Hytönen, Olli T. Pentikäinen, Susanna Repo, Mark S. Johnson, Markku S. Kulomaa |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Molecular model Ovalbumin Protein Conformation Clinical Biochemistry Crystallography X-Ray Ligands Sensitivity and Specificity Biochemistry Avian Proteins chemistry.chemical_compound Ultraviolet visible spectroscopy Biotin Drug Discovery Animals Molecular Biology Glycoproteins chemistry.chemical_classification Pharmacology Azo compound Binding Sites biology Calorimetry Differential Scanning Molecular Structure Stereoisomerism General Medicine Ligand (biochemistry) Avidin Combinatorial chemistry CHEMBIO chemistry Biotinylation biology.protein Molecular Medicine Spectrophotometry Ultraviolet Glycoprotein Azo Compounds Chickens |
| Zdroj: | Chemistry & Biology. (10):1029-1039 |
| ISSN: | 1074-5521 |
| DOI: | 10.1016/j.chembiol.2006.08.006 |
| Popis: | Summary 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 β3 and β4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 A) X-ray structure for avidin reported here. These results may be valuable in designing improved tools for avidin-based life science and nanobiotechnology applications. |
| Databáze: | OpenAIRE |
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