期刊
SCIENCE ADVANCES
卷 6, 期 29, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aba8161
关键词
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资金
- National Key Research and Development Program of China [2017YFA0504801, 2017YFA0504803, 2018YFA0507700]
- National Natural Science Foundation of China [91954119, 31870736, 31570750, 31870834]
- Fundamental Research Funds for the Central Universities [2018XZZX001-13]
Calcium homeostasis modulator 1 (CALHM1) is a voltage-gated ATP release channel that plays an important role in neural gustatory signaling and the pathogenesis of Alzheimer's disease. Here, we present a cryo-electron microscopy structure of full-length Ca2+-free CALHM1 from Danio rerio at an overall resolution of 3.1 angstrom. Our structure reveals an octameric architecture with a wide pore diameter of similar to 20 angstrom, presumably representing the active conformation. The overall structure is substantially different from that of the isoform CALHM2, which forms both undecameric hemichannels and gap junctions. The N-terminal small helix folds back to the pore and forms an antiparallel interaction with transmembrane helix 1. Structural analysis revealed that the extracellular loop 1 region within the dimer interface may contribute to oligomeric assembly. A positive potential belt inside the pore was identified that may modulate ion permeation. Our structure offers insights into the assembly and gating mechanism of the CALHM1 channel.
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