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Armadillo motifs involved in vesicular transport

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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 (U.S.A.)
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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