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Structure paper

TitleStructural bases of inhibitory mechanism of Ca1.2 channel inhibitors.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 2772, Year 2024
Publish dateMar 30, 2024
AuthorsYiqing Wei / Zhuoya Yu / Lili Wang / Xiaojing Li / Na Li / Qinru Bai / Yuhang Wang / Renjie Li / Yufei Meng / Hao Xu / Xianping Wang / Yanli Dong / Zhuo Huang / Xuejun Cai Zhang / Yan Zhao /
PubMed AbstractThe voltage-gated calcium channel Ca1.2 is essential for cardiac and vessel smooth muscle contractility and brain function. Accumulating evidence demonstrates that malfunctions of Ca1.2 are involved ...The voltage-gated calcium channel Ca1.2 is essential for cardiac and vessel smooth muscle contractility and brain function. Accumulating evidence demonstrates that malfunctions of Ca1.2 are involved in brain and heart diseases. Pharmacological inhibition of Ca1.2 is therefore of therapeutic value. Here, we report cryo-EM structures of Ca1.2 in the absence or presence of the antirheumatic drug tetrandrine or antihypertensive drug benidipine. Tetrandrine acts as a pore blocker in a pocket composed of S6, S6, and S6 helices and forms extensive hydrophobic interactions with Ca1.2. Our structure elucidates that benidipine is located in the D-D fenestration site. Its hydrophobic sidechain, phenylpiperidine, is positioned at the exterior of the pore domain and cradled within a hydrophobic pocket formed by S5, S6, and S6 helices, providing additional interactions to exert inhibitory effects on both L-type and T-type voltage gated calcium channels. These findings provide the structural foundation for the rational design and optimization of therapeutic inhibitors of voltage-gated calcium channels.
External linksNat Commun / PubMed:38555290 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.5 Å
Structure data

34880

8hlp

EMDB-34880, PDB-8hlp:
Cryo-EM structure of human high-voltage activated L-type calcium channel CaV1.2 (apo)
Method: EM (single particle) / Resolution: 3.5 Å

34891

8hma

EMDB-34891, PDB-8hma:
Cryo-EM structure of human high-voltage activated L-type calcium channel CaV1.2 in complex with tetrandrine (TET)
Method: EM (single particle) / Resolution: 3.4 Å

34892

8hmb

EMDB-34892, PDB-8hmb:
Cryo-EM structure of human high-voltage activated L-type calcium channel CaV1.2 in complex with benidipine (BEN)
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-R16:
HEXADECANE

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

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

PDB-1ac9:
SOLUTION STRUCTURE OF A DNA DECAMER CONTAINING THE ANTIVIRAL DRUG GANCICLOVIR: COMBINED USE OF NMR, RESTRAINED MOLECULAR DYNAMICS, AND FULL RELAXATION REFINEMENT, 6 STRUCTURES

ChemComp-BMA:
beta-D-mannopyranose

PDB-1ac8:
VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / apo state / tet bound state / ben bound state

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