9cuk

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Current revision (07:50, 21 November 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9cuk is ON HOLD until Paper Publication
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==Structure of human full-length derived TRPV6 channel in Calmodulin-bound state==
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<StructureSection load='9cuk' size='340' side='right'caption='[[9cuk]], [[Resolution|resolution]] 3.26&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9cuk]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CUK 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]] 3.26&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</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=9cuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cuk OCA], [https://pdbe.org/9cuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cuk RCSB], [https://www.ebi.ac.uk/pdbsum/9cuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cuk ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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TRPV6 is a Ca(2+) selective channel that mediates calcium uptake in the gut and contributes to the development and progression of human cancers. TRPV6 is represented by the ancestral and derived haplotypes that differ by three non-synonymous polymorphisms, located in the N-terminal ankyrin repeat domain (C157R), S1-S2 extracellular loop (M378V), and C-terminus (M681T). The ancestral and derived haplotypes were proposed to serve as genomic factors causing a different outcome for cancer patients of African ancestry. We solved cryoelectron microscopy (cryo-EM) structures of ancestral and derived TRPV6 in the open and calmodulin (CaM)-bound inactivated states. Neither state shows substantial structural differences caused by the non-synonymous polymorphisms. Functional properties assessed by electrophysiological recordings and Ca(2+) uptake measurements, and water and ion permeation evaluated by molecular modeling also appear similar between the haplotypes. Therefore, ancestral and derived TRPV6 have similar structure and function, implying that other factors are responsible for the differences in susceptibility to cancer.
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Authors:
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Structure-function analyses of human TRPV6 ancestral and derived haplotypes.,Neuberger A, Shalygin A, Trofimov YA, Veretenenko II, Nadezhdin KD, Krylov NA, Gudermann T, Efremov RG, Chubanov V, Sobolevsky AI Structure. 2024 Oct 28:S0969-2126(24)00453-2. doi: 10.1016/j.str.2024.10.018. PMID:39500315<ref>PMID:39500315</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9cuk" 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: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Nadezhdin KD]]
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[[Category: Neuberger A]]
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[[Category: Sobolevsky AI]]

Current revision

Structure of human full-length derived TRPV6 channel in Calmodulin-bound state

PDB ID 9cuk

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