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A Threonine Turnstile Defines a Dynamic Amphiphilic Binding Motif in the AAA ATPase p97 Allosteric Binding Site
The turnstile motion of two neighboring threonines sets up a dynamic side chain interplay that can accommodate both polar and apolar ligands in a small molecule allosteric protein binding site. A computational model based on SAR data and both X-ray and cryo-EM structures of the AAA ATPase p97 was us...
Tallennettuna:
| Julkaisussa: | Org Biomol Chem |
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| Päätekijät: | , , , , , , , , , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2017
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5472064/ https://ncbi.nlm.nih.gov/pubmed/28352916 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c7ob00526a |
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