1mfw

<table><tr><td colspan='2'>[[1mfw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MFW FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mg4|1mg4]], [[1mjd|1mjd]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mfw OCA], [http://pdbe.org/1mfw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mfw RCSB], [http://www.ebi.ac.uk/pdbsum/1mfw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mfw ProSAT]</span></td></tr>

[[http://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.

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== 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>

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<div class="pdbe-citations 1mfw" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Bushweller, J H]]

[[Category: Cierpickil, T]]

[[Category: Dauter, Z]]

[[Category: Derewenda, U]]

[[Category: Derewenda, Z]]

[[Category: Devedjiev, Y]]

[[Category: Feng, Y]]

[[Category: Kim, M H]]

[[Category: Krowarsch, D]]

[[Category: Otlewski, J]]

[[Category: Walsh, C A]]

[[Category: Transferase]]