9tyv | pdb_00009tyv
Cryo-EM Structure of Human TMEM45B
Structural highlights
FunctionTM45B_HUMAN Plays a role in innate immunity (PubMed:35938871). Mechanistically, promotes alphaviruses RNA degradation by interacting with the viral polymerase nsP4 and the mRNA-capping enzyme nsP1 and thereby interfering with the interaction between viral RNA and nsP1 (PubMed:35938871). Essential for inflammation- and tissue injury-induced mechanical pain hypersensitivity (By similarity).[UniProtKB:Q8VCZ2][1] Publication Abstract from PubMedThe orphan transmembrane protein 45B (TMEM45B) has been reported to be involved in mechanical pain hypersensitivity, antiviral processes, and cancer. The structure of human TMEM45B with bound monosialodihexosylganglioside (GM3, 18:1;O2/24:1), presented here, determined by single-particle cryo-electron microscopy (cryo-EM) to 2.8 A, reveals a homotetrameric assembly of seven-transmembrane-helix protomers. The first six transmembrane helices from each protomer create a central hydrophobic tunnel that accommodates metal ions and the C24:1 fatty acid component of the ganglioside GM3. Cryo-EM structure of human TMEM45B with a bound GM3 (18:1;O2/24:1).,Grieben M, Inderhees J, Ebersberger N J Struct Biol. 2026 Sep 24;218(4):108376. doi: 10.1016/j.jsb.2026.108376. PMID:42785650[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||