2i1j: Difference between revisions
New page: left|200px<br /><applet load="2i1j" size="350" color="white" frame="true" align="right" spinBox="true" caption="2i1j, resolution 2.10Å" /> '''Moesin from Spodopte... |
No edit summary |
||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
Ezrin/radixin/moesin (ERM) family members provide a regulated link between | 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 Structure== | ==About this Structure== | ||
| Line 14: | Line 14: | ||
[[Category: Spodoptera frugiperda]] | [[Category: Spodoptera frugiperda]] | ||
[[Category: Li, Q.]] | [[Category: Li, Q.]] | ||
[[Category: Nance, M | [[Category: Nance, M R.]] | ||
[[Category: Tesmer, J | [[Category: Tesmer, J J.G.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
| Line 32: | Line 32: | ||
[[Category: self-inhibition]] | [[Category: self-inhibition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:05 2008'' | ||
Revision as of 18:48, 21 February 2008
|
Moesin from Spodoptera frugiperda at 2.1 angstroms 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
2I1J 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
Page seeded by OCA on Thu Feb 21 17:48:05 2008