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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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1995
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC42129/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7724536/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.92.8.3180 |
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