ArticleNature communications2013
The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- The response of claudin-like transmembrane septate junction proteins to altered environmental ion levels in the larval mosquito Aedes aegypti.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2016Article
- Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization.Molecular biology of the cell · 2015Article
- The value of protein structure classification information-Surveying the scientific literature.Proteins · 2015Article
- Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1.Nature communications · 2015Article
- The kidney tight junction (Review).International journal of molecular medicine · 2014Review
- Epithelial adhesive junctions.F1000prime reports · 2014Review
- Claudin interactions in and out of the tight junction.Tissue barriers · 2013Review
- Highlighting membrane protein structure and function: A celebration of the Protein Data Bank.The Journal of biological chemistryReview
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Authors and funding
9 authors.
Funding
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Abstract
Euglenoid flagellates have striped surface structures comprising pellicles, which allow the cell shape to vary from rigid to flexible during the characteristic movement of the flagellates. In Euglena gracilis, the pellicular strip membranes are covered with paracrystalline arrays of a major integral membrane protein, IP39, a putative four-membrane-spanning protein with the conserved sequence motif of the PMP-22/EMP/MP20/Claudin superfamily. Here we report the three-dimensional structure of Euglena IP39 determined by electron crystallography. Two-dimensional crystals of IP39 appear to form a striated pattern of antiparallel double-rows in which trimeric IP39 units are longitudinally polymerised, resulting in continuously extending zigzag-shaped lines. Structural analysis revealed an asymmetric molecular arrangement in the trimer, and suggested that at least four different interactions between neighbouring protomers are involved. A combination of such multiple interactions would be important for linear strand formation of membrane proteins in a lipid bilayer.
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