Cryo-electron microscopy structure of the TRPV2 ion channel

Details

• Alternative Title:
  Nat Struct Mol Biol
• Personal Author:
  Zubcevic, Lejla ; Herzik, Mark A ; Chung, Ben C ; Liu, Zhirui ; Lander, Gabriel C ; Lee, Seok-Yong
• Description:
  Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ∼4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.
• Subjects:
  Animals Ankyrin Repeat Cryoelectron Microscopy Models, Molecular Protein Conformation Rabbits TRPV Cation Channels
• Source:
  Nat Struct Mol Biol. 23(2):180-186.
• Pubmed ID:
  26779611
• Pubmed Central ID:
  PMC4876856
• Document Type:
  Journal Article
• Funding:
  DP2 EB020402/EB/NIBIB NIH HHS/United States ; DP2 OD008380/OD/NIH HHS/United States ; DP2EB020402/DP/NCCDPHP CDC HHS/United States ; DP2OD008380/OD/NIH HHS/United States ; R01GM100894/GM/NIGMS NIH HHS/United States
• Volume:
  23
• Issue:
  2
• Collection(s):
  CDC Public Access
• Main Document Checksum:
  urn:sha256:9b82c8271cbd54c6f596f005077e711acdb002624535d451974af82d78076382
• Download URL:
  https://stacks.cdc.gov/view/cdc/39774/cdc_39774_DS1.pdf
• File Type:
  [PDF - 1.52 MB ]