2i1k: Difference between revisions

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New page: left|200px<br /><applet load="2i1k" size="350" color="white" frame="true" align="right" spinBox="true" caption="2i1k, resolution 3.000Å" /> '''Moesin from Spodopt...
 
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[[Image:2i1k.gif|left|200px]]<br /><applet load="2i1k" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2i1k, resolution 3.000&Aring;" />
'''Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution'''<br />


==Overview==
==Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution==
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.
<StructureSection load='2i1k' size='340' side='right'caption='[[2i1k]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<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>
<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>
</table>
== 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>


==About this Structure==
==See Also==
2I1K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=URE:'>URE</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1K OCA].
*[[Moesin|Moesin]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17134719 17134719]
[[Category: Large Structures]]
[[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: CL]]
[[Category: GOL]]
[[Category: URE]]
[[Category: actin binding]]
[[Category: c-ermad]]
[[Category: coiled-coil]]
[[Category: erm]]
[[Category: ezrin]]
[[Category: ferm]]
[[Category: masking]]
[[Category: merlin]]
[[Category: moesin]]
[[Category: radixin]]
[[Category: regulation]]
[[Category: self-inhibition]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:33:02 2008''

Latest revision as of 12:01, 21 February 2024

Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolutionMoesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution

Structural highlights

2i1k is a 1 chain structure with sequence from Spodoptera frugiperda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0T1L9_SPOFR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2i1k, resolution 3.00Å

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OCA
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