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...

Disgrifiad llawn

Wedi'i Gadw mewn:
Manylion Llyfryddiaeth
Cyhoeddwyd yn:Org Biomol Chem
Prif Awduron: 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
Fformat: Artigo
Iaith:Inglês
Cyhoeddwyd: 2017
Pynciau:
Article
Mynediad Ar-lein: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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