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6du8

From Proteopedia

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Current revision

Human Polycsytin 2-l1

6du8, resolution 3.11Å

Structural highlights

6du8 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	PKD2L1, PKD2L, PKDL, TRPP3 (HUMAN)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

We report the near atomic resolution (3.3 A) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1.

Cryo-EM structure of the polycystin 2-l1 ion channel.,Hulse RE, Li Z, Huang RK, Zhang J, Clapham DE Elife. 2018 Jul 13;7. pii: 36931. doi: 10.7554/eLife.36931. PMID:30004384^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chen XZ, Vassilev PM, Basora N, Peng JB, Nomura H, Segal Y, Brown EM, Reeders ST, Hediger MA, Zhou J. Polycystin-L is a calcium-regulated cation channel permeable to calcium ions. Nature. 1999 Sep 23;401(6751):383-6. PMID:10517637 doi:http://dx.doi.org/10.1038/43907
↑ Huque T, Cowart BJ, Dankulich-Nagrudny L, Pribitkin EA, Bayley DL, Spielman AI, Feldman RS, Mackler SA, Brand JG. Sour ageusia in two individuals implicates ion channels of the ASIC and PKD families in human sour taste perception at the anterior tongue. PLoS One. 2009 Oct 8;4(10):e7347. doi: 10.1371/journal.pone.0007347. PMID:19812697 doi:http://dx.doi.org/10.1371/journal.pone.0007347
↑ Yu Y, Ulbrich MH, Li MH, Dobbins S, Zhang WK, Tong L, Isacoff EY, Yang J. Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex. Nat Commun. 2012 Dec 4;3:1252. doi: 10.1038/ncomms2257. PMID:23212381 doi:http://dx.doi.org/10.1038/ncomms2257
↑ DeCaen PG, Delling M, Vien TN, Clapham DE. Direct recording and molecular identification of the calcium channel of primary cilia. Nature. 2013 Dec 12;504(7479):315-8. doi: 10.1038/nature12832. PMID:24336289 doi:http://dx.doi.org/10.1038/nature12832
↑ Hulse RE, Li Z, Huang RK, Zhang J, Clapham DE. Cryo-EM structure of the polycystin 2-l1 ion channel. Elife. 2018 Jul 13;7. pii: 36931. doi: 10.7554/eLife.36931. PMID:30004384 doi:http://dx.doi.org/10.7554/eLife.36931

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6du8"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6du8 is ON HOLD  until Jun 20 2020
+==Human Polycsytin 2-l1==
+<SX load='6du8' size='340' side='right' viewer='molstar' caption='[[6du8]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6du8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DU8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6DU8 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PKD2L1, PKD2L, PKDL, TRPP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6du8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6du8 OCA], [http://pdbe.org/6du8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6du8 RCSB], [http://www.ebi.ac.uk/pdbsum/6du8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6du8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We report the near atomic resolution (3.3 A) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1.
-Authors: Hulse, R.E., Clapham, D.E., Li, Z., Huang, R.K., Zhang, J.
+Cryo-EM structure of the polycystin 2-l1 ion channel.,Hulse RE, Li Z, Huang RK, Zhang J, Clapham DE Elife. 2018 Jul 13;7. pii: 36931. doi: 10.7554/eLife.36931. PMID:30004384<ref>PMID:30004384</ref>
-Description: Human Polycsytin 2-l1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6du8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Human]]
+[[Category: Large Structures]]
+[[Category: Clapham, D E]]
+[[Category: Huang, R K]]
+[[Category: Hulse, R E]]
 [[Category: Li, Z]]
-[[Category: Clapham, D.E]]
 [[Category: Zhang, J]]
-[[Category: Hulse, R.E]]
+[[Category: Membrane protein]]
-[[Category: Huang, R.K]]
+[[Category: Pc2l1]]
+[[Category: Pkd2l1]]
+[[Category: Polycystic 2-l1]]
+[[Category: Trpp2]]

6du8

From Proteopedia

Current revision

Human Polycsytin 2-l1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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