The golgin family gives identity and structure to the Golgi apparatus and is part of a complex protein network at the Golgi membrane. The golgin p115 is targeted by the GTPase Rab1a, contains a large globular head region and a long region of coiled-coil which forms an extended rod-like structure. p115 serves as vesicle tethering factor and plays an important role at different steps of vesicular transport. Here we present the 2.2 A-resolution X-ray structure of the globular head region of p115. The structure exhibits an armadillo fold that is decorated by elongated loops and carries a C-terminal non-canonical repeat. This terminal repeat folds into the armadillo superhelical groove and allows homodimeric association with important implications for p115 mediated multiple protein interactions and tethering.
Unusual armadillo fold in the human general vesicular transport factor p115.
人类通用囊泡运输因子 p115 中不寻常的犰狳褶皱
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作者:Striegl Harald, Roske Yvette, Kümmel Daniel, Heinemann Udo
| 期刊: | PLoS One | 影响因子: | 2.600 |
| 时间: | 2009 | 起止号: | 2009;4(2):e4656 |
| doi: | 10.1371/journal.pone.0004656 | 种属: | Human |
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