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Article

Crystal structure and characterization of coiled-coil domain of the transient receptor potential channel PKD2L1.

Biochimica et biophysica acta - 1 Mar 2012

Molland Katrina L, Paul Lake N, Yernool Dinesh A

Abstract excerpt

The cation-permeable channel PKD2L1 forms a homomeric assembly as well as heteromeric associations with both PKD1 and PKD1L3, with the cytoplasmic regulatory domain (CRD) of PKD2L1 often playing a role in assembly and/or function. Our previous work indicated that the isolated PKD2L1 CRD assembles as a trimer in a manner dependent on the presence of a proposed oligomerization domain. Herein we describe the 2.7Å...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 22193359
DOI: 10.1016/j.bbapap.2011.12.002

Genes

PKD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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