2xrp

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{{STRUCTURE_2xrp| PDB=2xrp | SCENE= }}
 
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===Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules===
 
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{{ABSTRACT_PUBMED_20974813}}
 
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==Disease==
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==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==
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[[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).
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<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xrp]] 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=2XRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.2&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [https://pdbe.org/2xrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [https://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Microtubule-associated proteins (MAPs) are essential for regulating and organizing cellular microtubules (MTs). However, our mechanistic understanding of MAP function is limited by a lack of detailed structural information. Using cryo-electron microscopy and single particle algorithms, we solved the 8 A structure of doublecortin (DCX)-stabilized MTs. Because of DCX's unusual ability to specifically nucleate and stabilize 13-protofilament MTs, our reconstruction provides unprecedented insight into the structure of MTs with an in vivo architecture, and in the absence of a stabilizing drug. DCX specifically recognizes the corner of four tubulin dimers, a binding mode ideally suited to stabilizing both lateral and longitudinal lattice contacts. A striking consequence of this is that DCX does not bind the MT seam. DCX binding on the MT surface indirectly stabilizes conserved tubulin-tubulin lateral contacts in the MT lumen, operating independently of the nucleotide bound to tubulin. DCX's exquisite binding selectivity uncovers important insights into regulation of cellular MTs.
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==Function==
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Template-free 13-protofilament microtubule-MAP assembly visualized at 8 A resolution.,Fourniol FJ, Sindelar CV, Amigues B, Clare DK, Thomas G, Perderiset M, Francis F, Houdusse A, Moores CA J Cell Biol. 2010 Nov 1;191(3):463-70. Epub 2010 Oct 25. PMID:20974813<ref>PMID:20974813</ref>
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[[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).
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2xrp]] 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=2XRP OCA].
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</div>
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<div class="pdbe-citations 2xrp" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Tubulin|Tubulin]]
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*[[Tubulin 3D Structures|Tubulin 3D Structures]]
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*[[Tubulin tyrosine ligase 3D structures|Tubulin tyrosine ligase 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:020974813</ref><references group="xtra"/><references/>
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<references/>
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__TOC__
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</SX>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Tubulin GTPase]]
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[[Category: Large Structures]]
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[[Category: Amigues, B.]]
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[[Category: Amigues B]]
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[[Category: Clare, D K.]]
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[[Category: Clare DK]]
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[[Category: Fourniol, F J.]]
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[[Category: Fourniol FJ]]
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[[Category: Francis, F.]]
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[[Category: Francis F]]
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[[Category: Houdusse, A.]]
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[[Category: Houdusse A]]
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[[Category: Moores, C A.]]
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[[Category: Moores CA]]
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[[Category: Perderiset, M.]]
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[[Category: Perderiset M]]
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[[Category: Sindelar, C V.]]
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[[Category: Sindelar CV]]
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[[Category: Thomas, G.]]
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[[Category: Thomas G]]
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[[Category: Structural protein]]
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Current revision

Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules

2xrp, resolution 8.20Å

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