1t3s

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[[Image:1t3s.jpg|left|200px]]
 
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==Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core==
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The line below this paragraph, containing "STRUCTURE_1t3s", creates the "Structure Box" on the page.
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<StructureSection load='1t3s' size='340' side='right'caption='[[1t3s]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1t3s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T3S FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#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=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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{{STRUCTURE_1t3s| PDB=1t3s | SCENE= }}
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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=1t3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3s OCA], [https://pdbe.org/1t3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t3s RCSB], [https://www.ebi.ac.uk/pdbsum/1t3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CACB2_RABIT CACB2_RABIT] The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t3/1t3s_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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</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=1t3s ConSurf].
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<div style="clear:both"></div>
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'''Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core'''
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Huntington's disease (HD) is initiated by an abnormally expanded polyglutamine stretch in the huntingtin protein, conferring a novel property on the protein that leads to the loss of striatal neurons. Defects in mitochondrial function have been implicated in the pathogenesis of HD. Here, we have examined the hypothesis that the mutant huntingtin protein may directly interact with the mitochondrion and affect its function. In human neuroblastoma cells and clonal striatal cells established from HdhQ7 (wild-type) and HdhQ111 (mutant) homozygote mouse knock-in embryos, huntingtin was present in a purified mitochondrial fraction. Subfractionation of the mitochondria and limited trypsin digestion of the organelle demonstrated that huntingtin was associated with the outer mitochondrial membrane. We further demonstrated that a recombinant truncated mutant huntingtin protein, but not a wild-type, directly induced mitochondrial permeability transition (MPT) pore opening in isolated mouse liver mitochondria, an effect that was prevented completely by cyclosporin A (CSA) and ATP. Importantly, the mutant huntingtin protein significantly decreased the Ca2+ threshold necessary to trigger MPT pore opening. We found a similar increased susceptibility to the calcium-induced MPT in liver mitochondria isolated from a knock-in HD mouse model. The mutant huntingtin protein-induced MPT pore opening was accompanied by a significant release of cytochrome c, an effect completely inhibited by CSA. These findings suggest that the development of specific MPT inhibitors may be an interesting therapeutic avenue to delay the onset of HD.
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[[Category: Large Structures]]
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==About this Structure==
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1T3S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3S OCA].
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==Reference==
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Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release., Choo YS, Johnson GV, MacDonald M, Detloff PJ, Lesort M, Hum Mol Genet. 2004 Jul 15;13(14):1407-20. Epub 2004 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15163634 15163634]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Campbell KP]]
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[[Category: Campbell, K P.]]
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[[Category: Chen C-C]]
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[[Category: Chen, C C.]]
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[[Category: Hirsch JA]]
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[[Category: Hirsch, J A.]]
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[[Category: Opatowsky Y]]
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[[Category: Opatowsky, Y.]]
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[[Category: Guanylate kinase domain]]
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[[Category: Sh3 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:29:16 2008''
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Current revision

Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core

PDB ID 1t3s

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