Unusual armadillo fold in the human general vesicular transport factor p115.

PLoS One

Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.

Published: April 2009

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2645507PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0004656PLOS

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