Article ; Online: TRPM7 reflected in Cryo-EMirror.
2018 Volume 76, Page(s) 129–131
Abstract: ... co-workers [1] published three TRPM7 structures resolved by cryo-electron microscopy (cryo-EM ... 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 ...
| 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. |
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| MeSH term(s) | Animals ; Calcium ; Cryoelectron Microscopy ; Homeostasis ; Humans ; Magnesium ; Protein-Serine-Threonine Kinases ; TRPM Cation Channels | |||||
| Chemical Substances | TRPM Cation Channels ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1) ; Magnesium (I38ZP9992A) ; Calcium (SY7Q814VUP) | |||||
| Language | English | |||||
| Publishing date | 2018-11-15 | |||||
| Publishing country | Netherlands | |||||
| Document type | Journal Article ; Research Support, Non-U.S. Gov't ; Comment | |||||
| ZDB-ID | 757687-0 | |||||
| ISSN | 1532-1991 ; 0143-4160 | |||||
| ISSN (online) | 1532-1991 | |||||
| ISSN | 0143-4160 | |||||
| DOI | 10.1016/j.ceca.2018.11.004 | |||||
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| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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