2emt: Difference between revisions

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-[[Image:2emt.png|left|200px]]
-<!--
+==Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1==
-The line below this paragraph, containing "STRUCTURE_2emt", creates the "Structure Box" on the page.
+<StructureSection load='2emt' size='340' side='right'caption='[[2emt]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2emt]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EMT FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=2emt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2emt OCA], [https://pdbe.org/2emt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2emt RCSB], [https://www.ebi.ac.uk/pdbsum/2emt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2emt ProSAT]</span></td></tr>
-{{STRUCTURE_2emt|  PDB=2emt  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
+== 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/em/2emt_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=2emt ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+P-selectin glycoprotein ligand-1 (PSGL-1), an adhesion molecule with O-glycosylated extracellular sialomucins, is involved in leukocyte inflammatory responses. On activation, ezrin-radixin-moesin (ERM) proteins mediate the redistribution of PSGL-1 on polarized cell surfaces to facilitate binding to target molecules. ERM proteins recognize a short binding motif, Motif-1, conserved in cytoplasmic tails of adhesion molecules, whereas PSGL-1 lacks Motif-1 residues important for binding to ERM proteins. The crystal structure of the complex between the radixin FERM domain and a PSGL-1 juxtamembrane peptide reveals that the peptide binds the groove of FERM subdomain C by forming a beta-strand associated with strand beta5C, followed by a loop flipped out towards the solvent. The Motif-1 3(10) helix present in the FERM-ICAM-2 complex is absent in PSGL-1 given the absence of a critical Motif-1 alanine residue, and PSGL-1 reduces its contact area with subdomain C. Non-conserved positions are occupied by large residues Met9 and His8, which stabilize peptide conformation and enhance groove binding. Non-conserved residues play an important role in compensating for loss of binding energy resulting from the absence of conserved residues important for binding.
-===Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1===
+Structural basis of PSGL-1 binding to ERM proteins.,Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T Genes Cells. 2007 Dec;12(12):1329-38. PMID:18076570<ref>PMID:18076570</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2emt" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18076570}}, adds the Publication Abstract to the page
+*[[Radixin|Radixin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18076570 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18076570}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[2emt]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EMT OCA].
-==Reference==
-<ref group="xtra">PMID:18076570</ref><ref group="xtra">PMID:17183174</ref><references group="xtra"/>
 [[Category: Mus musculus]]
-[[Category: Hakoshima, T.]]
+[[Category: Hakoshima T]]
-[[Category: Kitano, K.]]
+[[Category: Kitano K]]
-[[Category: Maesaki, R.]]
+[[Category: Maesaki R]]
-[[Category: Takai, Y.]]
+[[Category: Takai Y]]
-[[Category: Terawaki, S.]]
+[[Category: Terawaki S]]
-[[Category: Cell adhesion]]
-[[Category: Protein-peptide complex]]