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...

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Bibliographic Details
Published in:Org Biomol Chem
Main Authors: Burnett, James C., Lim, Chaemin, Peyser, Brian D., Samankumara, Lalith P., Kovaliov, Marina, Colombo, Raffaele, Bulfer, Stacie L., LaPorte, Matthew G., Hermone, Ann R., McGrath, Connor F., Arkin, Michelle R., Gussio, Rick, Huryn, Donna M., Wipf, Peter
Format: Artigo
Language:Inglês
Published: 2017
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Online Access: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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