Structural origins of high-affinity biotin binding to streptavidin.
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Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR
Structural origins of high-affinity biotin binding to streptavidin.
Science. 1989 Jan 6;243(4887):85-8.
- PubMed ID
- 2911722 [ View in PubMed]
- 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 beta sheets that link tetramer subunits.