Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin.

In natural streptavidin, tryptophan 120 of each subunit makes contacts with the biotin bound by an adjacent subunit through the dimer-dimer interface. To understand quantitatively the role of tryptophan 120 and its intersubunit communication in the properties of streptavidin, a streptavidin mutant i...

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Bibliographische Detailangaben
Hauptverfasser: Sano, T, Cantor, C R
Format: Artigo
Sprache:Inglês
Veröffentlicht: 1995
Schlagworte:
Research Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC42129/
https://ncbi.nlm.nih.gov/pubmed/7724536
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