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Crystal Structure of an antiparallel coiled-coil tetramerization domain from TRPM7 channelsCrystal Structure of an antiparallel coiled-coil tetramerization domain from TRPM7 channels
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTransient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. Earlier studies showed that members of the TRPM subclass possess a self-assembling tetrameric C-terminal cytoplasmic coiled-coil domain that underlies channel assembly and trafficking. Here, we present the high-resolution crystal structure of the coiled-coil domain of the channel enzyme TRPM7. The crystal structure, together with biochemical experiments, reveals an unexpected four-stranded antiparallel coiled-coil architecture that bears unique features relative to other antiparallel coiled-coils. Structural analysis indicates that a limited set of interactions encode assembly specificity determinants and uncovers a previously unnoticed segregation of TRPM assembly domains into two families that correspond with the phylogenetic divisions seen for the complete subunits. Together, the data provide a framework for understanding the mechanism of TRPM channel assembly and highlight the diversity of forms found in the coiled-coil fold. X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil.,Fujiwara Y, Minor DL Jr J Mol Biol. 2008 Nov 21;383(4):854-70. Epub 2008 Aug 29. PMID:18782578[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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