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2v71

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[[Image:2v71.gif|left|200px]]
 
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{{Structure
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==Coiled-coil region of NudEL==
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|PDB= 2v71 |SIZE=350|CAPTION= <scene name='initialview01'>2v71</scene>, resolution 2.24&Aring;
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<StructureSection load='2v71' size='340' side='right'caption='[[2v71]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[2v71]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V71 FirstGlance]. <br>
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|ACTIVITY=
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</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>
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|GENE=
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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=2v71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v71 OCA], [https://pdbe.org/2v71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v71 RCSB], [https://www.ebi.ac.uk/pdbsum/2v71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v71 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Evolutionary Conservation ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v71 OCA], [http://www.ebi.ac.uk/pdbsum/2v71 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v71 RCSB]</span>
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[[Image:Consurf_key_small.gif|200px|right]]
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}}
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Check<jmol>
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<jmolCheckbox>
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'''COILED-COIL REGION OF NUDEL'''
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v7/2v71_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Overview==
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</jmolCheckbox>
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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=2v71 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Ndel1 and Nde1 are homologous and evolutionarily conserved proteins, with critical roles in cell division, neuronal migration, and other physiological phenomena. These functions are dependent on their interactions with the retrograde microtubule motor dynein and with its regulator Lis1--a product of the causal gene for isolated lissencephaly sequence (ILS) and Miller-Dieker lissencephaly. The molecular basis of the interactions of Ndel1 and Nde1 with Lis1 is not known. Here, we present a crystallographic study of two fragments of the coiled-coil domain of Ndel1, one of which reveals contiguous high-quality electron density for residues 10-166, the longest such structure reported by X-ray diffraction at high resolution. Together with complementary solution studies, our structures reveal how the Ndel1 coiled coil forms a stable parallel homodimer and suggest mechanisms by which the Lis1-interacting domain can be regulated to maintain a conformation in which two supercoiled alpha helices cooperatively bind to a Lis1 homodimer.
Ndel1 and Nde1 are homologous and evolutionarily conserved proteins, with critical roles in cell division, neuronal migration, and other physiological phenomena. These functions are dependent on their interactions with the retrograde microtubule motor dynein and with its regulator Lis1--a product of the causal gene for isolated lissencephaly sequence (ILS) and Miller-Dieker lissencephaly. The molecular basis of the interactions of Ndel1 and Nde1 with Lis1 is not known. Here, we present a crystallographic study of two fragments of the coiled-coil domain of Ndel1, one of which reveals contiguous high-quality electron density for residues 10-166, the longest such structure reported by X-ray diffraction at high resolution. Together with complementary solution studies, our structures reveal how the Ndel1 coiled coil forms a stable parallel homodimer and suggest mechanisms by which the Lis1-interacting domain can be regulated to maintain a conformation in which two supercoiled alpha helices cooperatively bind to a Lis1 homodimer.
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==About this Structure==
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The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly.,Derewenda U, Tarricone C, Choi WC, Cooper DR, Lukasik S, Perrina F, Tripathy A, Kim MH, Cafiso DS, Musacchio A, Derewenda ZS Structure. 2007 Nov;15(11):1467-81. PMID:17997972<ref>PMID:17997972</ref>
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2V71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V71 OCA].
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==Reference==
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The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly., Derewenda U, Tarricone C, Choi WC, Cooper DR, Lukasik S, Perrina F, Tripathy A, Kim MH, Cafiso DS, Musacchio A, Derewenda ZS, Structure. 2007 Nov;15(11):1467-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17997972 17997972]
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[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Cooper, D R.]]
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[[Category: Derewenda, U.]]
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[[Category: Derewenda, Z S.]]
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[[Category: Kim, M H.]]
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[[Category: alternative splicing]]
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[[Category: coiled coil]]
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[[Category: cytoplasm]]
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[[Category: cytoskeleton]]
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[[Category: developmental protein]]
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[[Category: differentiation]]
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[[Category: lis1 binding]]
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[[Category: microtubule]]
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[[Category: microtubule associated migration]]
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[[Category: neurogenesis]]
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[[Category: nuclear protein]]
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[[Category: phosphorylation]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:00 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2v71" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Cooper, D R]]
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[[Category: Derewenda, U]]
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[[Category: Derewenda, Z S]]
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[[Category: Kim, M H]]
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[[Category: Cytoskeleton]]
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[[Category: Developmental protein]]
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[[Category: Differentiation]]
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[[Category: Lis1 binding]]
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[[Category: Microtubule]]
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[[Category: Microtubule associated migration]]
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[[Category: Neurogenesis]]
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[[Category: Nuclear protein]]
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[[Category: Phosphorylation]]
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[[Category: Transport]]

Current revision

Coiled-coil region of NudEL

PDB ID 2v71

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