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Structural Origins of High-Affinity Biotin Binding to Streptavidin

Weber, Patricia C., Ohlendorf, D. H., Wendoloski, J. J., Salemme, F. R.·1989·Science

Abstract

The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted β sheets that link tetramer subunits.

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Metadata

Authors
Weber, P. C., Ohlendorf, D. H., Wendoloski, J. J., & Salemme, F. R.
Venue
Science
Published
1989-01-06
Volume
243
Issue
4887
Pages
85-88
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2051654117
Cited by
1,223
References
0
FWCI
8.08
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural Origins of High-Affinity Biotin Binding to Streptavidin. https://app.cochat.ai/papers/10.1126/science.2911722
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Weber, P. C., Ohlendorf, D. H., Wendoloski, J. J., & Salemme, F. R. (1989). Structural Origins of High-Affinity Biotin Binding to Streptavidin. Science. https://doi.org/10.1126/science.2911722

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.