2d1l: Difference between revisions

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-{{Seed}}
-[[Image:2d1l.png|left|200px]]
-<!--
+==Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)==
-The line below this paragraph, containing "STRUCTURE_2d1l", creates the "Structure Box" on the page.
+<StructureSection load='2d1l' size='340' side='right'caption='[[2d1l]], [[Resolution|resolution]] 1.85&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'>[[2d1l]] is a 2 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=2D1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D1L 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]] 1.85&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_2d1l|  PDB=2d1l  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1l OCA], [https://pdbe.org/2d1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d1l RCSB], [https://www.ebi.ac.uk/pdbsum/2d1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d1l ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MTSS1_MOUSE MTSS1_MOUSE] Inhibits the nucleation of actin filaments in vitro.<ref>PMID:12482861</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/d1/2d1l_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2d1l ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The adaptor protein missing-in-metastasis (MIM) contains independent F- and G-actin binding domains, consisting, respectively, of an N-terminal 250 aa IRSp53/MIM homology domain (IMD) and a C-terminal WASP-homology domain 2 (WH2). We determined the crystal structures of MIM's IMD and that of its WH2 bound to actin. The IMD forms a dimer, with each subunit folded as an antiparallel three-helix bundle. This fold is related to that of the BAR domain. Like the BAR domain, the IMD has been implicated in membrane binding. Yet, comparison of the structures reveals that the membrane binding surfaces of the two domains have opposite curvatures, which may determine the type of curvature of the interacting membrane. The WH2 of MIM is longer than the prototypical WH2, interacting with all four subdomains of actin. We characterize a similar WH2 at the C terminus of IRSp53 and propose that in these two proteins WH2 performs a scaffolding function.
-===Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)===
+Structural basis for the actin-binding function of missing-in-metastasis.,Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R Structure. 2007 Feb;15(2):145-55. PMID:17292833<ref>PMID:17292833</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_17292833}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2d1l" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 17292833 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17292833}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-D1L is a 2 chains structure of sequences 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=2D1L OCA].
-==Reference==
-<ref group="xtra">PMID:17292833</ref><references group="xtra"/>
 [[Category: Mus musculus]]
-[[Category: Chereau, D.]]
+[[Category: Chereau D]]
-[[Category: Dominguez, R.]]
+[[Category: Dominguez R]]
-[[Category: Ferron, F.]]
+[[Category: Ferron F]]
-[[Category: Kerff, F.]]
+[[Category: Kerff F]]
-[[Category: Lee, S H.]]
+[[Category: Lee SH]]
-[[Category: Actin binding]]
-[[Category: Imd]]
-[[Category: Irsp53]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:31:25 2009''