1mg4: Difference between revisions

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 <StructureSection load='1mg4' size='340' side='right'caption='[[1mg4]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mg4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MG4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mg4]] is a 1 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=1MG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MG4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.504&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mfw|1mfw]], [[1mjd|1mjd]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1mg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mg4 OCA], [https://pdbe.org/1mg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mg4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/DCLK1_HUMAN DCLK1_HUMAN]] Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
+[https://www.uniprot.org/uniprot/DCLK1_HUMAN DCLK1_HUMAN] Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1mg4 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The doublecortin-like domains (DCX), which typically occur in tandem, are novel microtubule-binding modules. DCX tandems are found in doublecortin, a 360-residue protein expressed in migrating neurons; the doublecortin-like kinase (DCLK); the product of the RP1 gene that is responsible for a form of inherited blindness; and several other proteins. Mutations in the gene encoding doublecortin cause lissencephaly in males and the 'double-cortex syndrome' in females. We here report a solution structure of the N-terminal DCX domain of human doublecortin and a 1.5 A resolution crystal structure of the equivalent domain from human DCLK. Both show a stable, ubiquitin-like tertiary fold with distinct structural similarities to GTPase-binding domains. We also show that the C-terminal DCX domains of both proteins are only partially folded. In functional assays, the N-terminal DCX domain of doublecortin binds only to assembled microtubules, whereas the C-terminal domain binds to both microtubules and unpolymerized tubulin.
-The DCX-domain tandems of doublecortin and doublecortin-like kinase.,Kim MH, Cierpicki T, Derewenda U, Krowarsch D, Feng Y, Devedjiev Y, Dauter Z, Walsh CA, Otlewski J, Bushweller JH, Derewenda ZS Nat Struct Biol. 2003 May;10(5):324-33. PMID:12692530<ref>PMID:12692530</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mg4" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bushweller, J H]]
+[[Category: Bushweller JH]]
-[[Category: Cierpickil, T]]
+[[Category: Cierpickil T]]
-[[Category: Dauter, Z]]
+[[Category: Dauter Z]]
-[[Category: Derewenda, U]]
+[[Category: Derewenda U]]
-[[Category: Derewenda, Z]]
+[[Category: Derewenda Z]]
-[[Category: Devedjiev, Y]]
+[[Category: Devedjiev Y]]
-[[Category: Feng, Y]]
+[[Category: Feng Y]]
-[[Category: Kim, M H]]
+[[Category: Kim MH]]
-[[Category: Krowarsch, D]]
+[[Category: Krowarsch D]]
-[[Category: Otlewski, J]]
+[[Category: Otlewski J]]
-[[Category: Walsh, C A]]
+[[Category: Walsh CA]]
-[[Category: Cortex development]]
-[[Category: Dcx domain]]
-[[Category: Doublecortin-like kinase]]
-[[Category: Microtubule bundling]]
-[[Category: Transferase]]