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4U46

Crystal structure of an avidin mutant

Summary for 4U46
Entry DOI10.2210/pdb4u46/pdb
DescriptorAvidin, CHLORIDE ION (3 entities in total)
Functional Keywordsavidin, biotin, ligand binding, sterols, biotin binding protein
Biological sourceGallus gallus (Chicken)
Cellular locationSecreted: P02701
Total number of polymer chains2
Total formula weight32153.00
Authors
Agrawal, N.,Lehtonen, S.,Kahkonen, N.,Riihimaki, T.,Hytonen, V.P.,Kulomaa, M.S.,Johnson, M.S.,Airenne, T.T. (deposition date: 2014-07-23, release date: 2015-08-05, Last modification date: 2023-12-20)
Primary citationLehtonen, S.I.,Tullila, A.,Agrawal, N.,Kukkurainen, S.,Kahkonen, N.,Koskinen, M.,Nevanen, T.K.,Johnson, M.S.,Airenne, T.T.,Kulomaa, M.S.,Riihimaki, T.A.,Hytonen, V.P.
Artificial Avidin-Based Receptors for a Panel of Small Molecules.
Acs Chem.Biol., 11:211-221, 2016
Cited by
PubMed Abstract: Proteins with high specificity, affinity, and stability are needed for biomolecular recognition in a plethora of applications. Antibodies are powerful affinity tools, but they may also suffer from limitations such as low stability and high production costs. Avidin and streptavidin provide a promising scaffold for protein engineering, and due to their ultratight binding to D-biotin they are widely used in various biotechnological and biomedical applications. In this study, we demonstrate that the avidin scaffold is suitable for use as a novel receptor for several biologically active small molecules: Artificial, chicken avidin-based proteins, antidins, were generated using a directed evolution method for progesterone, hydrocortisone, testosterone, cholic acid, ketoprofen, and folic acid, all with micromolar to nanomolar affinity and significantly reduced biotin-binding affinity. We also describe the crystal structure of an antidin, sbAvd-2(I117Y), a steroid-binding avidin, which proves that the avidin scaffold can tolerate significant modifications without losing its characteristic tetrameric beta-barrel structure, helping us to further design avidin-based small molecule receptors.
PubMed: 26550684
DOI: 10.1021/acschembio.5b00906
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

226707

數據於2024-10-30公開中

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