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| Item Type: | Article |
|---|---|
| Title: | Armadillo motifs involved in vesicular transport |
| Creators Name: | Striegl, H. and Andrade-Navarro, M.A. and Heinemann, U. |
| Abstract: | Armadillo (ARM) repeat proteins function in various cellular processes including vesicular transport and membrane tethering. They contain an imperfect repeating sequence motif that forms a conserved three-dimensional structure. Recently, structural and functional insight into tethering mediated by the ARM-repeat protein p115 has been provided. Here we describe the p115 ARM-motifs for reasons of clarity and nomenclature and show that both sequence and structure are highly conserved among ARM-repeat proteins. We argue that there is no need to invoke repeat types other than ARM repeats for a proper description of the structure of the p115 globular head region. Additionally, we propose to define a new subfamily of ARM-like proteins and show lack of evidence that the ARM motifs found in p115 are present in other long coiled-coil tethering factors of the golgin family. |
| Keywords: | Amino Acid Motifs, Amino Acid Sequence, Armadillo Domain Proteins, Biological Transport, X-Ray Crystallography, Molecular Models, Molecular Sequence Data, Protein Multimerization, Secondary Protein Structure, Tertiary Protein Structure, Amino Acid Repetitive Sequences, Amino Acid Sequence Homology, Transport Vesicles, Vesicular Transport Proteins |
| Source: | PLoS ONE |
| ISSN: | 1932-6203 |
| Publisher: | Public Library of Science |
| Volume: | 5 |
| Number: | 2 |
| Page Range: | e8991 |
| Date: | 1 February 2010 |
| Official Publication: | https://doi.org/10.1371/journal.pone.0008991 |
| PubMed: | View item in PubMed |
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