1ni2

From Proteopedia

(Difference between revisions)

Current revision

Structure of the active FERM domain of Ezrin

Structural highlights

1ni2 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EZRI_HUMAN Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis.^[1] ^[2] ^[3]

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 PubMed

Ezrin is a member of the ERM (ezrin, radixin, moesin) family of proteins that cross-link the actin cytoskeleton to the plasma membrane and also may function in signaling cascades that regulate the assembly of actin stress fibers. Here, we report a crystal structure for the free (activated) FERM domain (residues 2-297) of recombinant human ezrin at 2.3 A resolution. Structural comparison among the dormant moesin FERM domain structure and the three known active FERM domain structures (radixin, moesin, and now ezrin) allows the clear definition of regions that undergo structural changes during activation. The key regions affected are residues 135-150 and 155-180 in lobe F2 and residues 210-214 and 235-267 in lobe F3. Furthermore, we show that a large increase in the mobilities of lobes F2 and F3 accompanies activation, suggesting that their integrity is compromised. This leads us to propose a new concept that we refer to as keystone interactions. Keystone interactions occur when one protein (or protein part) contributes residues that allow another protein to complete folding, meaning that it becomes an integral part of the structure and would rarely dissociate. Such interactions are well suited for long-lived cytoskeletal protein interactions. The keystone interactions concept leads us to predict two specific docking sites within lobes F2 and F3 that are likely to bind target proteins.

Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.,Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA J Biol Chem. 2003 Feb 14;278(7):4949-56. Epub 2002 Nov 11. PMID:12429733^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ D'Angelo R, Aresta S, Blangy A, Del Maestro L, Louvard D, Arpin M. Interaction of ezrin with the novel guanine nucleotide exchange factor PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in epithelial cells. Mol Biol Cell. 2007 Dec;18(12):4780-93. Epub 2007 Sep 19. PMID:17881735 doi:http://dx.doi.org/E06-12-1144
↑ Wald FA, Oriolo AS, Mashukova A, Fregien NL, Langshaw AH, Salas PJ. Atypical protein kinase C (iota) activates ezrin in the apical domain of intestinal epithelial cells. J Cell Sci. 2008 Mar 1;121(Pt 5):644-54. doi: 10.1242/jcs.016246. Epub 2008 Feb, 12. PMID:18270268 doi:10.1242/jcs.016246
↑ Austermann J, Nazmi AR, Heil A, Fritz G, Kolinski M, Filipek S, Gerke V. Generation and characterization of a novel, permanently active S100P mutant. Biochim Biophys Acta. 2009 Jun;1793(6):1078-85. doi:, 10.1016/j.bbamcr.2008.11.012. Epub 2008 Dec 8. PMID:19111582 doi:http://dx.doi.org/10.1016/j.bbamcr.2008.11.012
↑ Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA. Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions. J Biol Chem. 2003 Feb 14;278(7):4949-56. Epub 2002 Nov 11. PMID:12429733 doi:10.1074/jbc.M210601200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ni2"

@@ Line 1: / Line 1: @@
 ==Structure of the active FERM domain of Ezrin==
-<StructureSection load='1ni2' size='340' side='right' caption='[[1ni2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='1ni2' size='340' side='right'caption='[[1ni2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ni2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ni2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NI2 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VIL2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ni2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni2 PDBsum]</span></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=1ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni2 OCA], [https://pdbe.org/1ni2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ni2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ni2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ni2 ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EZRI_HUMAN EZRI_HUMAN] Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis.<ref>PMID:17881735</ref> <ref>PMID:18270268</ref> <ref>PMID:19111582</ref>
 == 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/ni/1ni2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ni/1ni2_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1ni2 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 24: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ni2" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 32: / Line 36: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bretscher, A P.]]
+[[Category: Large Structures]]
-[[Category: Cerione, R A.]]
+[[Category: Bretscher AP]]
-[[Category: Karplus, P A.]]
+[[Category: Cerione RA]]
-[[Category: Nassar, N.]]
+[[Category: Karplus PA]]
-[[Category: Smith, W J.]]
+[[Category: Nassar N]]
-[[Category: Acyl-coa-like domain]]
+[[Category: Smith WJ]]
-[[Category: Ferm]]
-[[Category: Keystone]]
-[[Category: Ph/ptb-like domain]]
-[[Category: Structural protein]]
-[[Category: Ubiquitin-like domain]]

1ni2

From Proteopedia

Current revision

Structure of the active FERM domain of Ezrin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox