1vyo
From Proteopedia
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| - | [[Image:1vyo.gif|left|200px]]<br /><applet load="1vyo" size=" | + | [[Image:1vyo.gif|left|200px]]<br /><applet load="1vyo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vyo, resolution 1.48Å" /> | caption="1vyo, resolution 1.48Å" /> | ||
'''CRYSTAL STRUCTURE OF AVIDIN'''<br /> | '''CRYSTAL STRUCTURE OF AVIDIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VYO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1VYO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:24:12 2008'' |
Revision as of 11:24, 23 January 2008
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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 with as ligand. Known structural/functional Site: . 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
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