7d7e

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Current revision (06:12, 21 November 2024) (edit) (undo)
 
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==Structure of PKD1L3-CTD/PKD2L1 in apo state==
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<StructureSection load='7d7e' size='340' side='right'caption='[[7d7e]]' scene=''>
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<StructureSection load='7d7e' size='340' side='right'caption='[[7d7e]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7d7e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D7E FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7d7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d7e OCA], [https://pdbe.org/7d7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d7e RCSB], [https://www.ebi.ac.uk/pdbsum/7d7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d7e ProSAT]</span></td></tr>
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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]] 3.4&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7d7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d7e OCA], [https://pdbe.org/7d7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d7e RCSB], [https://www.ebi.ac.uk/pdbsum/7d7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d7e ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PK2L1_MOUSE PK2L1_MOUSE] Pore-forming subunit of a ciliary calcium channel that controls calcium concentration within primary cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with PKD1L1 in primary cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and GLI2 transcription. May act as a sour taste receptor by forming a calcium channel with PKD1L3 in gustatory cells; however, its contribution to sour taste perception is unclear in vivo and may be indirect. May play a role in the perception of carbonation taste.<ref>PMID:15548533</ref> <ref>PMID:16891422</ref> <ref>PMID:16929298</ref> <ref>PMID:19833970</ref> <ref>PMID:21098668</ref> <ref>PMID:21625513</ref> <ref>PMID:24336288</ref> <ref>PMID:24336289</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The heteromeric complex between PKD1L3, a member of the polycystic kidney disease (PKD) protein family, and PKD2L1, also known as TRPP2 or TRPP3, has been a prototype for mechanistic characterization of heterotetrametric TRP-like channels. Here we show that a truncated PKD1L3/PKD2L1 complex with the C-terminal TRP-fold fragment of PKD1L3 retains both Ca(2+) and acid-induced channel activities. Cryo-EM structures of this core heterocomplex with or without supplemented Ca(2+) were determined at resolutions of 3.1 A and 3.4 A, respectively. The heterotetramer, with a pseudo-symmetric TRP architecture of 1:3 stoichiometry, has an asymmetric selectivity filter (SF) guarded by Lys2069 from PKD1L3 and Asp523 from the three PKD2L1 subunits. Ca(2+)-entrance to the SF vestibule is accompanied by a swing motion of Lys2069 on PKD1L3. The S6 of PKD1L3 is pushed inward by the S4-S5 linker of the nearby PKD2L1 (PKD2L1-III), resulting in an elongated intracellular gate which seals the pore domain. Comparison of the apo and Ca(2+)-loaded complexes unveils an unprecedented Ca(2+) binding site in the extracellular cleft of the voltage-sensing domain (VSD) of PKD2L1-III, but not the other three VSDs. Structure-guided mutagenic studies support this unconventional site to be responsible for Ca(2+)-induced channel activation through an allosteric mechanism.
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Structural basis for Ca(2+) activation of the heteromeric PKD1L3/PKD2L1 channel.,Su Q, Chen M, Wang Y, Li B, Jing D, Zhan X, Yu Y, Shi Y Nat Commun. 2021 Aug 11;12(1):4871. doi: 10.1038/s41467-021-25216-z. PMID:34381056<ref>PMID:34381056</ref>
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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 7d7e" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Mus musculus]]
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[[Category: Chen M]]
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[[Category: Jing D]]
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[[Category: Li B]]
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[[Category: Shi Y]]
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[[Category: Su Q]]
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[[Category: Wang Y]]
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[[Category: Yu Y]]
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[[Category: Zhan X]]

Current revision

Structure of PKD1L3-CTD/PKD2L1 in apo state

PDB ID 7d7e

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