2i1j: Difference between revisions
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|PDB= 2i1j |SIZE=350|CAPTION= <scene name='initialview01'>2i1j</scene>, resolution 2.10Å | |PDB= 2i1j |SIZE=350|CAPTION= <scene name='initialview01'>2i1j</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=URE:UREA'>URE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1isn|1ISN]], [[1j19|1J19]], [[1e5w|1E5W]], [[1sgh|1SGH]], [[1ef1|1EF1]], [[1gc6|1GC6]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1j OCA], [http://www.ebi.ac.uk/pdbsum/2i1j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i1j RCSB]</span> | |||
}} | }} | ||
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[[Category: Nance, M R.]] | [[Category: Nance, M R.]] | ||
[[Category: Tesmer, J J.G.]] | [[Category: Tesmer, J J.G.]] | ||
[[Category: actin binding]] | [[Category: actin binding]] | ||
[[Category: c-ermad]] | [[Category: c-ermad]] | ||
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[[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 Mon Mar 31 03:38:24 2008'' | ||
Revision as of 03:38, 31 March 2008
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| , resolution 2.10Å | |||||||
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| Ligands: | , , | ||||||
| Related: | 1ISN, 1J19, 1E5W, 1SGH, 1EF1, 1GC6
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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