NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway.

ABSTRACT: As an AAA-ATPase, Vps4 is important for function of multivesicular bodies (MVB) sorting pathway, which involves in cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. The activity of Vps4 is stimulated by the interactions between Vta1 N-terminus (named as Vta1NTD) and Did2 fragment (176-204 aa) (termed as Did2_176-204) or Vps60 (128-186 aa) (termed as Vps60_128-186). The structural basis of how Vta1NTD binds to Did2_176-204 is still unclear. To address this, in this report, the structure of Did2_176-204 in complex with Vta1NTD was determined by NMR techniques, demonstrating that Did2_176-204 interacts with Vta1NTD through its helix α6' extending over the 2^nd and the 3^rd α-helices o

SUBMITTER: Shen J 

PROVIDER: S-EPMC5141497 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature