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Inactive conformation enhances binding function in physiological conditions
Many receptors display conformational flexibility, in which the binding pocket has an open inactive conformation in the absence of ligand and a tight active conformation when bound to ligand. Here we study the bacterial adhesin FimH to address the role of the inactive conformation of the pocket for...
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| 出版年: | Proc Natl Acad Sci U S A |
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| 主要な著者: | , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
2015
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4538629/ https://ncbi.nlm.nih.gov/pubmed/26216967 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1503160112 |
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