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| Item Type: | Article |
|---|---|
| Title: | Unusual armadillo fold in the human general vesicular transport factor p115 |
| Creators Name: | Striegl, H., Roske, Y., Kuemmel, D. and Heinemann, U. |
| Abstract: | 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. |
| Keywords: | Amino Acid Sequence, X-Ray Crystallography, Molecular Models, Molecular Sequence Data, Protein Conformation, Protein Folding, Amino Acid Sequence Homology, Vesicular Transport Proteins |
| Source: | PLoS ONE |
| ISSN: | 1932-6203 |
| Publisher: | Public Library of Science |
| Volume: | 4 |
| Number: | 2 |
| Page Range: | e4656 |
| Date: | 27 February 2009 |
| Official Publication: | https://doi.org/10.1371/journal.pone.0004656 |
| PubMed: | View item in PubMed |
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