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Structure paper

TitleStructures of the R-type human Ca2.3 channel reveal conformational crosstalk of the intracellular segments.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 7358, Year 2022
Publish dateNov 30, 2022
AuthorsXia Yao / Yan Wang / Zhifei Wang / Xiao Fan / Di Wu / Jian Huang / Alexander Mueller / Sarah Gao / Miaohui Hu / Carol V Robinson / Yong Yu / Shuai Gao / Nieng Yan /
PubMed AbstractThe R-type voltage-gated Ca (Ca) channels Ca2.3, widely expressed in neuronal and neuroendocrine cells, represent potential drug targets for pain, seizures, epilepsy, and Parkinson's disease. Despite ...The R-type voltage-gated Ca (Ca) channels Ca2.3, widely expressed in neuronal and neuroendocrine cells, represent potential drug targets for pain, seizures, epilepsy, and Parkinson's disease. Despite their physiological importance, there have lacked selective small-molecule inhibitors targeting these channels. High-resolution structures may aid rational drug design. Here, we report the cryo-EM structure of human Ca2.3 in complex with α2δ-1 and β3 subunits at an overall resolution of 3.1 Å. The structure is nearly identical to that of Ca2.2, with VSD in the down state and the other three VSDs up. A phosphatidylinositol 4,5-bisphosphate (PIP2) molecule binds to the interface of VSD and the tightly closed pore domain. We also determined the cryo-EM structure of a Ca2.3 mutant in which a Ca2-unique cytosolic helix in repeat II (designated the CH2 helix) is deleted. This mutant, named ΔCH2, still reserves a down VSD, but PIP2 is invisible and the juxtamembrane region on the cytosolic side is barely discernible. Our structural and electrophysiological characterizations of the wild type and ΔCH2 Ca2.3 show that the CH2 helix stabilizes the inactivated conformation of the channel by tightening the cytosolic juxtamembrane segments, while CH2 helix is not necessary for locking the down state of VSD.
External linksNat Commun / PubMed:36446785 / PubMed Central
MethodsEM (single particle)
Resolution3.1 Å
Structure data

28529

8epl

EMDB-28529, PDB-8epl:
Human R-type voltage-gated calcium channel Cav2.3 at 3.1 Angstrom resolution
Method: EM (single particle) / Resolution: 3.1 Å

28530

8epm

EMDB-28530, PDB-8epm:
Human R-type voltage-gated calcium channel Cav2.3 CH2II-deleted mutant at 3.1 Angstrom resolution
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

ChemComp-PT5:
[(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho / phospholipid*YM / Phosphatidylinositol 4,5-bisphosphate

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Cav2.3 / Channels / Calcium Ion-Selective

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