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| [[Image:2i1k.gif|left|200px]]
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| {{Structure
| | ==Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution== |
| |PDB= 2i1k |SIZE=350|CAPTION= <scene name='initialview01'>2i1k</scene>, resolution 3.000Å
| | <StructureSection load='2i1k' size='340' side='right'caption='[[2i1k]], [[Resolution|resolution]] 3.00Å' scene=''> |
| |SITE= | | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=URE:UREA'>URE</scene>
| | <table><tr><td colspan='2'>[[2i1k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I1K FirstGlance]. <br> |
| |ACTIVITY=
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| |GENE=
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=URE:UREA'>URE</scene></td></tr> |
| |DOMAIN=
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1k OCA], [https://pdbe.org/2i1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i1k RCSB], [https://www.ebi.ac.uk/pdbsum/2i1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i1k ProSAT]</span></td></tr> |
| |RELATEDENTRY=[[1isn|1ISN]], [[1j19|1J19]], [[1e5w|1E5W]], [[1sgh|1SGH]], [[1ef1|1EF1]], [[1gc6|1GC6]], [[2i1j|2I1J]]
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1k OCA], [http://www.ebi.ac.uk/pdbsum/2i1k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i1k RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/A0T1L9_SPOFR A0T1L9_SPOFR] |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/2i1k_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2i1k ConSurf]. |
| | <div style="clear:both"></div> |
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| '''Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution'''
| | ==See Also== |
| | | *[[Moesin|Moesin]] |
| | | __TOC__ |
| ==Overview==
| | </StructureSection> |
| 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.
| | [[Category: Large Structures]] |
| | |
| ==About this Structure== | |
| 2I1K is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1K OCA].
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| ==Reference==
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| 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]
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| [[Category: Protein complex]] | |
| [[Category: Spodoptera frugiperda]] | | [[Category: Spodoptera frugiperda]] |
| [[Category: Nance, M R.]] | | [[Category: Nance MR]] |
| [[Category: Tesmer, J J.G.]] | | [[Category: Tesmer JJG]] |
| [[Category: actin binding]]
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| [[Category: c-ermad]]
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| [[Category: coiled-coil]]
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| [[Category: erm]]
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| [[Category: ezrin]]
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| [[Category: ferm]]
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| [[Category: masking]]
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| [[Category: merlin]]
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| [[Category: moesin]]
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| [[Category: radixin]]
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| [[Category: regulation]]
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| [[Category: self-inhibition]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:24 2008''
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