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How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer

Abstract:

The interaction between SA (streptavidin) and biotin is one of the strongest non-covalent interactions in Nature. SA is a widely used tool and a paradigm for protein-ligand interactions. We previously developed a SA mutant, termed Tr (treptavidin), possessing a 10-fold lower off-rate for biotin, with increased mechanical and thermal stability. In the present study, we determined the crystal structures of apo-Tr at 1.5 Å resolution. In apo-SA the loop (L3/4), near biotin's valeryl tail, is typ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1042/BJ20101593

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More from this funder
Funding agency for:
Koner, A
Grant:
085457/Z/OB/Z
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Funding agency for:
Howarth, M
Grant:
085457/Z/OB/Z
More from this funder
Funding agency for:
Lowe, E
Publisher:
Portland Press Ltd. Publisher's website
Journal:
Biochemical Journal Journal website
Volume:
435
Pages:
55-63
Publication date:
2011-01-01
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
Language:
English
Keywords:
Subjects:
UUID:
uuid:8a51a274-44f6-4d0d-b41a-4a26d96215e0
Local pid:
ora:5990
Deposit date:
2012-01-06

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