1mg4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1mg4' size='340' side='right'caption='[[1mg4]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1mg4' size='340' side='right'caption='[[1mg4]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1mg4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.504Å</td></tr> |
- | <tr id=' | + | <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> | <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> | </table> | ||
== Function == | == 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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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]. | </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="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. | ||
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- | 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> | ||
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- | From MEDLINE®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Bushweller | + | [[Category: Bushweller JH]] |
- | [[Category: Cierpickil | + | [[Category: Cierpickil T]] |
- | [[Category: Dauter | + | [[Category: Dauter Z]] |
- | [[Category: Derewenda | + | [[Category: Derewenda U]] |
- | [[Category: Derewenda | + | [[Category: Derewenda Z]] |
- | [[Category: Devedjiev | + | [[Category: Devedjiev Y]] |
- | [[Category: Feng | + | [[Category: Feng Y]] |
- | [[Category: Kim | + | [[Category: Kim MH]] |
- | [[Category: Krowarsch | + | [[Category: Krowarsch D]] |
- | [[Category: Otlewski | + | [[Category: Otlewski J]] |
- | [[Category: Walsh | + | [[Category: Walsh CA]] |
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Current revision
STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: WILD TYPE PROTEIN
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Categories: Homo sapiens | Large Structures | Bushweller JH | Cierpickil T | Dauter Z | Derewenda U | Derewenda Z | Devedjiev Y | Feng Y | Kim MH | Krowarsch D | Otlewski J | Walsh CA