| Literature DB >> 30470536 |
Vladimir Chubanov1, Lorenz Mittermeier2, Thomas Gudermann3.
Abstract
TRPM7 is an atypical type of ion channel because its pore-forming moiety is covalently linked to a protein kinase domain. The channel-kinase TRPM7 controls a wide range of biological processes such as mineral homeostasis, immune responses, cell motility, proliferation and differentiation. Earlier this year, Duan J & co-workers [1] published three TRPM7 structures resolved by cryo-electron microscopy (cryo-EM). This study tremendously advances our mechanistic understanding of TRPM7 channel function and forms the basis for informed structure-function assessment of this extraordinary protein.Entities:
Keywords: Magnesium; TRP channels; TRPM2; TRPM6; TRPM7
Mesh:
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Year: 2018 PMID: 30470536 DOI: 10.1016/j.ceca.2018.11.004
Source DB: PubMed Journal: Cell Calcium ISSN: 0143-4160 Impact factor: 6.817