Structural origins of high-affinity biotin binding to streptavidin

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

Research output: Contribution to journalArticlepeer-review

976 Scopus citations

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 indude 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.

Original languageEnglish (US)
Pages (from-to)85-88
Number of pages4
JournalScience
Volume243
Issue number4887
DOIs
StatePublished - Jan 1 1989
Externally publishedYes

Fingerprint Dive into the research topics of 'Structural origins of high-affinity biotin binding to streptavidin'. Together they form a unique fingerprint.

Cite this