2i1j: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='2i1j' size='340' side='right'caption='[[2i1j]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2i1j' size='340' side='right'caption='[[2i1j]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i1j]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2i1j]] 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=2I1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I1J FirstGlance]. <br> | ||
</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> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1isn|1isn]], [[1j19|1j19]], [[1e5w|1e5w]], [[1sgh|1sgh]], [[1ef1|1ef1]], [[1gc6|1gc6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1isn|1isn]], [[1j19|1j19]], [[1e5w|1e5w]], [[1sgh|1sgh]], [[1ef1|1ef1]], [[1gc6|1gc6]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1j OCA], [https://pdbe.org/2i1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i1j RCSB], [https://www.ebi.ac.uk/pdbsum/2i1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i1j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 27: | Line 27: | ||
</div> | </div> | ||
<div class="pdbe-citations 2i1j" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2i1j" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Moesin|Moesin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:24, 12 January 2022
Moesin from Spodoptera frugiperda at 2.1 angstroms resolutionMoesin from Spodoptera frugiperda at 2.1 angstroms resolution
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEzrin/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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||