Structural invariance of constitutively active and inactive mutants of Acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states

The three single-headed monomeric myosin I isozymes of Acanthamoeba castellanii (AMIs)—AMIA, AMIB, and AMIC—are among the best-studied of all myosins. We have used AMIC to study structural correlates of myosin’s actin-activated ATPase. This activity is normally controlled by phosphorylation of Ser-3...

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Autors principals: Carragher, Bridget O., Cheng, Naiqian, Wang, Zhen-Yuan, Korn, Edward D., Reilein, Amy, Belnap, David M., Hammer, John A., Steven, Alasdair C.
Format: Artigo
Idioma:Inglês
Publicat: The National Academy of Sciences 1998
Matèries:
Biological Sciences
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC28021/
https://ncbi.nlm.nih.gov/pubmed/9860947
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