Binding Properties of HABA-Type Azo Derivatives to Avidin and Avidin-Related Protein 4
نویسندگان
چکیده
منابع مشابه
Chicken avidin-related proteins show altered biotin-binding and physico-chemical properties as compared with avidin.
Chicken avidin and bacterial streptavidin are proteins familiar from their use in various (strept)avidin-biotin technological applications. Avidin binds the vitamin biotin with the highest affinity known for non-covalent interactions found in nature. The gene encoding avidin (AVD) has homologues in chicken, named avidin-related genes (AVRs). In the present study we used the AVR genes to produce...
متن کاملAvidin related protein 2 shows unique structural and functional features among the avidin protein family
BACKGROUND The chicken avidin gene family consists of avidin and several avidin related genes (AVRs). Of these gene products, avidin is the best characterized and is known for its extremely high affinity for D-biotin, a property that is utilized in numerous modern life science applications. Recently, the AVR genes have been expressed as recombinant proteins, which have shown different biotin-bi...
متن کاملThe structure of the complex between avidin and the dye, 2-(4'-hydroxyazobenzene) benzoic acid (HABA).
The crystal structure of the complex formed between the egg-white biotin-binding protein, avidin, and the dye, 2-(4'-hydroxyazobenzene) benzoic acid (HABA), was determined to a resolution of 2.5 A. The interaction of avidin with the benzoate ring of HABA is essentially identical to that of the complex formed between HABA and streptavidin (the bacterial analogue of the egg-white protein). This i...
متن کاملA Spectrophotometric Assay for Avidin and Biotin Based on Binding of Dyes by Avidin.
The binding of aniohic dyes by serum albumin has been studied by many workers (reviewed by Foster, 1960). The evidence suggests several cationic sites situated in hydrophobic regions of the molecule. For example, the bound dye shows spectral changes that are in accord with its location in a non-polar environment. Since it was suggested (Green, 1963b) that the biotin-binding sites of avidin were...
متن کاملThree-dimensional structures of avidin and the avidin-biotin complex.
The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its complex with biotin have been determined to 2.6 and 3.0 A, respectively. The structures reveal the amino acid residues critical for stabilization of the tetrameric assembly and for the exceptionally tight binding of biotin. Each monomer is an eight-stranded antiparallel beta-barrel, remarkably simila...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 2006
ISSN: 1074-5521
DOI: 10.1016/j.chembiol.2006.08.006