4atu: Difference between revisions

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==Human doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM map of doublecortin-stabilised microtubules reconstructed in absence of kinesin==
==Human doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM map of doublecortin-stabilised microtubules reconstructed in absence of kinesin==
<StructureSection load='4atu' size='340' side='right' caption='[[4atu]], [[Resolution|resolution]] 8.30&Aring;' scene=''>
<SX load='4atu' size='340' side='right' viewer='molstar' caption='[[4atu]], [[Resolution|resolution]] 8.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4atu]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ATU FirstGlance]. <br>
<table><tr><td colspan='2'>[[4atu]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ATU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jff|1jff]], [[1mjd|1mjd]], [[1sa0|1sa0]], [[1sa1|1sa1]], [[1tvk|1tvk]], [[1z2b|1z2b]], [[2bqq|2bqq]], [[2wbe|2wbe]], [[2xrp|2xrp]], [[4aqv|4aqv]], [[4aqw|4aqw]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </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=4atu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atu OCA], [https://pdbe.org/4atu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4atu RCSB], [https://www.ebi.ac.uk/pdbsum/4atu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4atu ProSAT]</span></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=4atu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4atu RCSB], [http://www.ebi.ac.uk/pdbsum/4atu PDBsum]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Defects in DCX are the cause of lissencephaly X-linked type 1 (LISX1) [MIM:[http://omim.org/entry/300067 300067]]; also called X-LIS or LIS. LISX1 is a classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.<ref>PMID:9489699</ref> <ref>PMID:9489700</ref> <ref>PMID:9668176</ref> <ref>PMID:9817918</ref> <ref>PMID:11468322</ref> <ref>PMID:12552055</ref>  Defects in DCX are the cause of subcortical band heterotopia X-linked (SBHX) [MIM:[http://omim.org/entry/300067 300067]]; also known as double cortex or subcortical laminar heterotopia (SCLH). SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.<ref>PMID:9618162</ref> <ref>PMID:9989615</ref> <ref>PMID:10369164</ref> <ref>PMID:10441340</ref> <ref>PMID:10807542</ref> <ref>PMID:11601509</ref> <ref>PMID:11175293</ref> <ref>PMID:12390976</ref>  Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). [[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration.<ref>PMID:22359282</ref>  [[http://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).  
[https://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4atu" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tubulin|Tubulin]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Tubulin GTPase]]
[[Category: Large Structures]]
[[Category: Fourniol, F J]]
[[Category: Fourniol FJ]]
[[Category: Fu, X]]
[[Category: Fu X]]
[[Category: Houdusse, A]]
[[Category: Houdusse A]]
[[Category: Jaiswal, J K]]
[[Category: Jaiswal JK]]
[[Category: Liu, J S]]
[[Category: Liu JS]]
[[Category: Moores, C A]]
[[Category: Moores CA]]
[[Category: Schubert, C R]]
[[Category: Schubert CR]]
[[Category: Stultz, C M]]
[[Category: Stultz CM]]
[[Category: Walsh, C A]]
[[Category: Walsh CA]]
[[Category: Hydrolase]]
[[Category: Microtubule-associated protein]]

Latest revision as of 13:53, 9 May 2024

Human doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM map of doublecortin-stabilised microtubules reconstructed in absence of kinesinHuman doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM map of doublecortin-stabilised microtubules reconstructed in absence of kinesin

4atu, resolution 8.30Å

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