Structural, thermodynamic, and kinetic effects of a phosphomimetic mutation in dynein light chain LC8.

ABSTRACT: Dynein light chain LC8 is a small, dimeric, very highly conserved globular protein first identified as an integral part of the dynein and myosin molecular motors but now recognized as a dimerization hub with wider significance. Phosphorylation at Ser88 is thought to be involved in regulating LC8 in the apoptotic pathway. The phosphomimetic Ser88Glu mutation weakens dimerization of LC8 and thus its overall ligand-binding affinity, because only the dimer binds ligands. The 1.9 A resolution crystal structure of dimeric LC8(S88E) bound to a fragment of the ligand Swallow (Swa) presented here shows that the tertiary structure is identical to that of wild-type LC8/Swa, with Glu88 well accommodated sterically at the dimer interface. NMR longitudinal magnetization exchange spectroscopy reveals rem

SUBMITTER: Benison G 

PROVIDER: S-EPMC2821902 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature