1t0h: Difference between revisions

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{{Seed}}
[[Image:1t0h.png|left|200px]]


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==Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a==
The line below this paragraph, containing "STRUCTURE_1t0h", creates the "Structure Box" on the page.
<StructureSection load='1t0h' size='340' side='right'caption='[[1t0h]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1t0h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0H FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
{{STRUCTURE_1t0h|  PDB=1t0h  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0h OCA], [https://pdbe.org/1t0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0h RCSB], [https://www.ebi.ac.uk/pdbsum/1t0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0h ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t0/1t0h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1t0h ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Voltage-gated calcium channels (Ca(V)s) govern muscle contraction, hormone and neurotransmitter release, neuronal migration, activation of calcium-dependent signalling cascades, and synaptic input integration. An essential Ca(V) intracellular protein, the beta-subunit (Ca(V)beta), binds a conserved domain (the alpha-interaction domain, AID) between transmembrane domains I and II of the pore-forming alpha(1) subunit and profoundly affects multiple channel properties such as voltage-dependent activation, inactivation rates, G-protein modulation, drug sensitivity and cell surface expression. Here, we report the high-resolution crystal structures of the Ca(V)beta2a conserved core, alone and in complex with the AID. Previous work suggested that a conserved region, the beta-interaction domain (BID), formed the AID-binding site; however, this region is largely buried in the Ca(V)beta core and is unavailable for protein-protein interactions. The structure of the AID-Ca(V)beta2a complex shows instead that Ca(V)beta2a engages the AID through an extensive, conserved hydrophobic cleft (named the alpha-binding pocket, ABP). The ABP-AID interaction positions one end of the Ca(V)beta near the intracellular end of a pore-lining segment, called IS6, that has a critical role in Ca(V) inactivation. Together, these data suggest that Ca(V)betas influence Ca(V) gating by direct modulation of IS6 movement within the channel pore.


===Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a===
Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain.,Van Petegem F, Clark KA, Chatelain FC, Minor DL Jr Nature. 2004 Jun 10;429(6992):671-5. Epub 2004 May 12. PMID:15141227<ref>PMID:15141227</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1t0h" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15141227}}, adds the Publication Abstract to the page
*[[Ion channels 3D structures|Ion channels 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15141227 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15141227}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1T0H is a [[Protein complex]] structure of sequences 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=1T0H OCA].
 
==Reference==
Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain., Van Petegem F, Clark KA, Chatelain FC, Minor DL Jr, Nature. 2004 Jun 10;429(6992):671-5. Epub 2004 May 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15141227 15141227]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Chatelain, F.]]
[[Category: Chatelain F]]
[[Category: Clark, K.]]
[[Category: Clark K]]
[[Category: Jr., D Minor.]]
[[Category: Minor Jr D]]
[[Category: Petegem, F Van.]]
[[Category: Van Petegem F]]
[[Category: Nucleotide kinase like domain]]
[[Category: Sh3 domain]]
 
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