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TitleCryo-EM structure of the human TACAN in a closed state.
Journal, issue, pagesCell Rep, Vol. 38, Issue 9, Page 110445, Year 2022
Publish dateMar 1, 2022
AuthorsXiaozhe Chen / Yaojie Wang / Yang Li / Xuhang Lu / Jianan Chen / Ming Li / Tianlei Wen / Ning Liu / Shenghai Chang / Xing Zhang / Xue Yang / Yuequan Shen /
PubMed AbstractTACAN is an ion channel-like protein that may be involved in sensing mechanical pain. Here, we present the cryo-electron microscopic structure of human TACAN (hTACAN). hTACAN forms a dimer in which ...TACAN is an ion channel-like protein that may be involved in sensing mechanical pain. Here, we present the cryo-electron microscopic structure of human TACAN (hTACAN). hTACAN forms a dimer in which each protomer consists of a transmembrane globular domain (TMD) containing six helices and an intracellular domain (ICD) containing two helices. Molecular dynamic simulations suggest that each protomer contains a putative ion conduction pore. A single-point mutation of the key residue Met207 greatly increases membrane pressure-activated currents. In addition, each hTACAN subunit binds one cholesterol molecule. Our data show the molecular assembly of hTACAN and suggest that wild-type hTACAN is in a closed state.
External linksCell Rep / PubMed:35235791
MethodsEM (single particle)
Resolution3.66 Å
Structure data

31482

7f6v

EMDB-31482, PDB-7f6v:
Cryo-EM structure of the human TACAN channel in a closed state
Method: EM (single particle) / Resolution: 3.66 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / dimer

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