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Avidin
From Proteopedia
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The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin may account for its higher affinity constant. | The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin may account for its higher affinity constant. | ||
| - | Unexpectedly, a residual N-acetylglucosamine moiety was detected in the deglycosylated avidin monomer. These <scene name=' | + | Unexpectedly, a residual N-acetylglucosamine moiety was detected in the deglycosylated avidin monomer. These <scene name='41/410356/Cv/14'>sugars</scene> appear along with the biotin but outside of the biotin binding pockets. |
See also:<br /> | See also:<br /> | ||
Revision as of 13:16, 12 January 2016
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3D structures of Avidin
Updated on 12-January-2016
Reference
- Livnah O, Bayer EA, Wilchek M, Sussman JL. Three-dimensional structures of avidin and the avidin-biotin complex. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5076-80. PMID:8506353
- Livnah O, Bayer EA, Wilchek M, Sussman JL. The structure of the complex between avidin and the dye, 2-(4'-hydroxyazobenzene) benzoic acid (HABA). FEBS Lett. 1993 Aug 9;328(1-2):165-8. PMID:8344421
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Marcin Jozef Suskiewicz, Jaime Prilusky
