Ontology highlight
ABSTRACT:
SUBMITTER: Chen YN
PROVIDER: S-EPMC5368074 | biostudies-literature | 2017 Apr
REPOSITORIES: biostudies-literature
Chen Yan-Na YN Gu Xin X Zhou X Edward XE Wang Weidong W Cheng Dandan D Ge Yinghua Y Ye Fei F Xu H Eric HE Lv Zhengbing Z
Protein science : a publication of the Protein Society 20170301 4
TBC1D15 belongs to the TBC (Tre-2/Bub2/Cdc16) domain family and functions as a GTPase-activating protein (GAP) for Rab GTPases. So far, the structure of TBC1D15 or the TBC1D15·Rab complex has not been determined, thus, its catalytic mechanism on Rab GTPases is still unclear. In this study, we solved the crystal structures of the Shark and Sus TBC1D15 GAP domains, to 2.8 Å and 2.5 Å resolution, respectively. Shark-TBC1D15 and Sus-TBC1D15 belong to the same subfamily of TBC domain-containing prote ...[more]