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'''Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution''' | '''Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution''' | ||
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==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1K OCA]. | |||
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/17134719 17134719] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17134719 17134719] | ||
[[Category: Nance, M R.]] | [[Category: Nance, M R.]] | ||
[[Category: Tesmer, J J.G.]] | [[Category: Tesmer, J J.G.]] | ||
[[Category: | [[Category: Actin binding]] | ||
[[Category: | [[Category: C-ermad]] | ||
[[Category: | [[Category: Coiled-coil]] | ||
[[Category: | [[Category: Erm]] | ||
[[Category: | [[Category: Ezrin]] | ||
[[Category: | [[Category: Ferm]] | ||
[[Category: | [[Category: Masking]] | ||
[[Category: | [[Category: Merlin]] | ||
[[Category: | [[Category: Moesin]] | ||
[[Category: | [[Category: Radixin]] | ||
[[Category: | [[Category: Regulation]] | ||
[[Category: | [[Category: Self-inhibition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:57:56 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 06:57, 4 May 2008
Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution
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
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 Page seeded by OCA on Sun May 4 06:57:56 2008