Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Schindl, R; Romanin, C.
Assembly domains in TRP channels.
Biochem Soc Trans. 2007; 35(Pt 1): 84-85.
Doi: 10.1042/BST0350084
Web of Science
PubMed
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- Führende Autor*innen der Med Uni Graz
- Schindl Rainer
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- Abstract:
- The large family of mammalian TRP (transient receptor potential) ion channels encompasses diverse sensory functions. TRP proteins consist of six transmembrane domains, with a pore-loop motif between the fifth and sixth domains and cytosolic N- and C-termini. The intracellular strands not only interact with various proteins and lipids, but also include essential multimerization regions. This review summarizes the current knowledge of the intrinsic assembly domains that assure tetrameric TRP channel formation.
- Find related publications in this database (using NLM MeSH Indexing)
- Amino Acid Motifs -
- Animals -
- Ankyrins - chemistry
- Calcium Channels - chemistry
- Cytosol - metabolism
- Drosophila -
- Humans -
- Models, Biological -
- Protein Binding -
- Protein Structure, Tertiary -
- TRPC Cation Channels - chemistry
- TRPC Cation Channels - physiology
- TRPV Cation Channels - chemistry
- Find related publications in this database (Keywords)
- ankyrin repeat
- assembly domain
- coiled-coil domain
- tetramer
- transient receptor potential channel (TRP channel)
- transmembrane domain