1vyo
From Proteopedia
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[[Image:1vyo.gif|left|200px]] | [[Image:1vyo.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF AVIDIN''' | '''CRYSTAL STRUCTURE OF AVIDIN''' | ||
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[[Category: Johnson, M S.]] | [[Category: Johnson, M S.]] | ||
[[Category: Salminen, T A.]] | [[Category: Salminen, T A.]] | ||
- | [[Category: | + | [[Category: Biotin]] |
- | [[Category: | + | [[Category: Glycoprotein]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:55:25 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:55, 3 May 2008
CRYSTAL STRUCTURE OF AVIDIN
Overview
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 beta3 and beta4 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.
About this Structure
1VYO is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4., Repo S, Paldanius TA, Hytonen VP, Nyholm TK, Halling KK, Huuskonen J, Pentikainen OT, Rissanen K, Slotte JP, Airenne TT, Salminen TA, Kulomaa MS, Johnson MS, Chem Biol. 2006 Oct;13(10):1029-39. PMID:17052607 Page seeded by OCA on Sat May 3 12:55:25 2008