4gif

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Current revision (11:30, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4gif]] is a 1 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=4GIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GIF FirstGlance]. <br>
<table><tr><td colspan='2'>[[4gif]] is a 1 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=4GIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GIF 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=4gif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gif OCA], [https://pdbe.org/4gif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gif RCSB], [https://www.ebi.ac.uk/pdbsum/4gif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gif 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">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=4gif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gif OCA], [https://pdbe.org/4gif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gif RCSB], [https://www.ebi.ac.uk/pdbsum/4gif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gif ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/PK2L1_HUMAN PK2L1_HUMAN] 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.<ref>PMID:10517637</ref> <ref>PMID:19812697</ref> <ref>PMID:23212381</ref> <ref>PMID:24336289</ref>
[https://www.uniprot.org/uniprot/PK2L1_HUMAN PK2L1_HUMAN] 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.<ref>PMID:10517637</ref> <ref>PMID:19812697</ref> <ref>PMID:23212381</ref> <ref>PMID:24336289</ref>
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== Publication Abstract from PubMed ==
 
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Polycystic kidney disease (PKD) family proteins associate with transient receptor potential (TRP) channel family proteins to form functionally important complexes. PKD proteins differ from known ion channel-forming proteins and are generally thought to act as membrane receptors. Here we find that PKD1L3, a PKD protein, functions as a channel-forming subunit in an acid-sensing heteromeric complex formed by PKD1L3 and TRPP3, a TRP channel protein. Single amino-acid mutations in the putative pore region of both proteins alter the channel's ion selectivity. The PKD1L3/TRPP3 complex in the plasma membrane of live cells contains one PKD1L3 and three TRPP3. A TRPP3 C-terminal coiled-coil domain forms a trimer in solution and in crystal, and has a crucial role in the assembly and surface expression of the PKD1L3/TRPP3 complex. These results demonstrate that PKD subunits constitute a new class of channel-forming proteins, enriching our understanding of the function of PKD proteins and PKD/TRPP complexes.
 
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Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex.,Yu Y, Ulbrich MH, Li MH, Dobbins S, Zhang WK, Tong L, Isacoff EY, Yang J Nat Commun. 2012 Dec 4;3:1252. doi: 10.1038/ncomms2257. PMID:23212381<ref>PMID:23212381</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 4gif" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>

Current revision

C-terminal coiled-coil domain of transient receptor potential channel TRPP3 (PKD2L1, Polycystin-L)

PDB ID 4gif

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