8RLM: TRIF Oligomerisation

TRIF Oligomerisation. Determined by electron microscopy at 3.5 Å resolution. Released 16 Jul 2025.

Method
Electron microscopy
Resolution
3.5 Å
Organism
Homo sapiens
Chains
6
Atoms
7,434
Mol. weight
465.55 kDa
Released
16 Jul 2025

Explore 8RLM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8RLM contains 60 α-helices and 30 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, B, C, D, E and F: 10 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand395-40061
α-helix403-4053
α-helix406-41914
β-strand42611
α-helix427-4304
α-helix442-4476
β-strand449-45571
α-helix458-4603
α-helix463-47816
β-strand487-49041
α-helix496-4983
α-helix501-5066
β-strand513-51421
α-helix520-5278
α-helix530-55324

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TIR domain-containing adapter molecule 1A, B, C, D, E, Fprotein721Homo sapiensQ8IUC6 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>8RLM_1 TIR domain-containing adapter molecule 1 (chains A, B, C, D, E, F)
SNAMACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEA
RISLEALKADAVARLVARQWAGVDSTEDPEEPPDVSWAVARLYHLLAEEKLCPASLRDVA
YQEAVRTLSSRDDHRLGELQDEARNRCGWDIAGDPGSIRTLQSNLGCLPPSSALPSGTRS
LPRPIDGVSDWSQGCSLRSTGSPASLASNLEISQSPTMPFLSLHRSPHGPSKLCDDPQAS
LVPEPVPGGCQEPEEMSWPPSGEIASPPELPSSPPPGLPEVAPDATSTGLPDTPAAPETS
TNYPVECTEGSAGPQSLPLPILEPVENPCSVKDQTPLQLSVEDTTSPNTKPCPPTPTTPE
TSPPPPPPPPSSTPCSAHLTPSSLFPSSLESSSEQKFYNFVILHARADEHIALRVREKLE
ALGVPDGATFCEDFQVPGRGELSCLQDAIDHSAFIILLLTSNFDCRLSLHQVNQAMMSNL
TRQGSPDCVIPFLPLESSPAQLSSDTASLLSGLVRLDEHSQIFARKVANTFKPHRLQARK
AMWRKEQDTRALREQSQHLDGERMQAAALNAAYSAYLQSYLSYQAQMEQLQVAFGSHMSF
GTGAPYGARMPFGGQVPLGAPPPFPTWPGCPQPPPLHAWQAGTPPPPSPQPAAFPQSLPF
PQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQEAEHHHHH
H

Primary citation

Toll-like receptor signaling outcome is determined by the stoichiometry of the endogenous TRIFosome. Moncrieffe, M.C., Suresh, P., Boyle, J. et al. Sci Adv (2026) 12:eaeb9507-eaeb9507. DOI 10.1126/sciadv.aeb9507 · PubMed

Other PDB entries of the same protein (UniProt Q8IUC6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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