5iwk

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Structure of Transient Receptor Potential (TRP) channel TRPV6

Structural highlights

5iwk is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.247Å
Ligands:CA, DTB
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRPV6_RAT Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).[UniProtKB:Q91WD2][UniProtKB:Q9H1D0][1]

Publication Abstract from PubMed

Precise regulation of calcium homeostasis is essential for many physiological functions. The Ca(2+)-selective transient receptor potential (TRP) channels TRPV5 and TRPV6 play vital roles in calcium homeostasis as Ca(2+) uptake channels in epithelial tissues. Detailed structural bases for their assembly and Ca(2+) permeation remain obscure. Here we report the crystal structure of rat TRPV6 at 3.25 A resolution. The overall architecture of TRPV6 reveals shared and unique features compared with other TRP channels. Intracellular domains engage in extensive interactions to form an intracellular 'skirt' involved in allosteric modulation. In the K(+) channel-like transmembrane domain, Ca(2+) selectivity is determined by direct coordination of Ca(2+) by a ring of aspartate side chains in the selectivity filter. On the basis of crystallographically identified cation-binding sites at the pore axis and extracellular vestibule, we propose a Ca(2+) permeation mechanism. Our results provide a structural foundation for understanding the regulation of epithelial Ca(2+) uptake and its role in pathophysiology.

Crystal structure of the epithelial calcium channel TRPV6.,Saotome K, Singh AK, Yelshanskaya MV, Sobolevsky AI Nature. 2016 Jun 13;534(7608):506-11. doi: 10.1038/nature17975. PMID:27296226[2]

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

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Citations
38 reviews cite this structure
Understand spiciness: mechanism of TRPV1 channel activation by capsaicin.
Yang et al. (2017)
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See Also

References

  1. ↑ Yue L, Peng JB, Hediger MA, Clapham DE. CaT1 manifests the pore properties of the calcium-release-activated calcium channel. Nature. 2001 Apr 5;410(6829):705-9. PMID:11287959 doi:http://dx.doi.org/10.1038/35070596
  2. ↑ Saotome K, Singh AK, Yelshanskaya MV, Sobolevsky AI. Crystal structure of the epithelial calcium channel TRPV6. Nature. 2016 Jun 13;534(7608):506-11. doi: 10.1038/nature17975. PMID:27296226 doi:http://dx.doi.org/10.1038/nature17975

Contents


PDB ID 5iwk

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