2i1k
Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution
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OverviewOverview
Ezrin/radixin/moesin (ERM) family members provide a regulated link between, the cortical actin cytoskeleton and the plasma membrane to govern membrane, structure and organization. Here, we report the crystal structure of, intact insect moesin, revealing that its essential yet previously, uncharacterized alpha-helical domain forms extensive interactions with, conserved surfaces of the band four-point-one/ezrin/radixin/moesin (FERM), domain. These interdomain contacts provide a functional explanation for, how PIP(2) binding and tyrosine phosphorylation of ezrin lead to, activation, and provide an understanding of previously enigmatic, loss-of-function missense mutations in the tumor suppressor merlin., Sequence conservation and biochemical results indicate that this structure, represents a complete model for the closed state of all ERM-merlin, proteins, wherein the central alpha-helical domain is an active, participant in an extensive set of inhibitory interactions that can be, unmasked, in a rheostat-like manner, by coincident regulatory factors that, help determine cell polarity and membrane structure.
About this StructureAbout this Structure
2I1K is a Protein complex structure of sequences from Spodoptera frugiperda with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain., Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ, J Mol Biol. 2007 Feb 2;365(5):1446-59. Epub 2006 Oct 26. PMID:17134719
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