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Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2)

Abstract:

Mutations in either polycystin-1 (PC1 or PKD1) or polycystin-2 (PC2, PKD2 or TRPP1) cause autosomal-dominant polycystic kidney disease (ADPKD) through unknown mechanisms. Here we present the structure of human PC2 in a closed conformation, solved by electron cryomicroscopy at 4.2-Å resolution. The structure reveals a novel polycystin-specific 'tetragonal opening for polycystins' (TOP) domain tightly bound to the top of a classic transient receptor potential (TRP) channel structure. The TOP do...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

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Publisher copy:
10.1038/nsmb.3343

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Department:
Oxford, MSD, NDM, Structural Genomics Consortium
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Department:
Oxford, MSD, NDM, Structural Genomics Consortium
More by this author
Department:
Oxford, MSD, NDM, Structural Genomics Consortium
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Department:
Oxford, MSD, Pharmacology
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Department:
Oxford, MSD, Pharmacology
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Funding agency for:
Sitsapesan, R
Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Structural and Molecular Biology Journal website
Volume:
24
Issue:
2
Pages:
114–122
Publication date:
2016-12-19
DOI:
EISSN:
1545-9985
ISSN:
1545-9993
Pubs id:
pubs:666790
URN:
uri:77bb905e-786d-46df-b614-d574073dc037
UUID:
uuid:77bb905e-786d-46df-b614-d574073dc037
Local pid:
pubs:666790

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