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TitleStructures and gating mechanism of human TRPM2.
Journal, issue, pagesScience, Vol. 362, Issue 6421, Year 2018
Publish dateDec 21, 2018
AuthorsLongfei Wang / Tian-Min Fu / Yiming Zhou / Shiyu Xia / Anna Greka / Hao Wu /
PubMed AbstractTransient receptor potential (TRP) melastatin 2 (TRPM2) is a cation channel associated with numerous diseases. It has a C-terminal NUDT9 homology (NUDT9H) domain responsible for binding adenosine ...Transient receptor potential (TRP) melastatin 2 (TRPM2) is a cation channel associated with numerous diseases. It has a C-terminal NUDT9 homology (NUDT9H) domain responsible for binding adenosine diphosphate (ADP)-ribose (ADPR), and both ADPR and calcium (Ca) are required for TRPM2 activation. Here we report cryo-electron microscopy structures of human TRPM2 alone, with ADPR, and with ADPR and Ca NUDT9H forms both intra- and intersubunit interactions with the N-terminal TRPM homology region (MHR1/2/3) in the apo state but undergoes conformational changes upon ADPR binding, resulting in rotation of MHR1/2 and disruption of the intersubunit interaction. The binding of Ca further engages transmembrane helices and the conserved TRP helix to cause conformational changes at the MHR arm and the lower gating pore to potentiate channel opening. These findings explain the molecular mechanism of concerted TRPM2 gating by ADPR and Ca and provide insights into the gating mechanism of other TRP channels.
External linksScience / PubMed:30467180 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 6.36 Å
Structure data

9132

6mix

EMDB-9132, PDB-6mix:
Human TRPM2 ion channel in apo state
Method: EM (single particle) / Resolution: 3.6 Å

9133

6miz

EMDB-9133, PDB-6miz:
Human TRPM2 ion channel in an ADPR-bound state
Method: EM (single particle) / Resolution: 6.1 Å

9134

6mj2

EMDB-9134, PDB-6mj2:
Human TRPM2 ion channel in a calcium- and ADPR-bound state
Method: EM (single particle) / Resolution: 6.36 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Channel / TRPM2 / TRP / ADPR / ADP-ribose / NUDT9H / NUDT9 / calcium / ion channel

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