Cryo-EM structure of RIG-I bound to the internal sites of OHSLR30 (+ATP). Determined by electron microscopy at 2.9 Å resolution. Released 16 Nov 2022.
Explore 8DVU in 3D Show helices and sheets RCSB PDB PDBe
8DVU contains 30 α-helices and 25 β-strands across 1 chain. 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 245-250 | 6 | |
| α-helix | 254-256 | 3 | |
| β-strand | 260-261 | 2 | 1 |
| α-helix | 270-283 | 14 | |
| β-strand | 293-296 | 4 | 1 |
| α-helix | 300-314 | 15 | |
| β-strand | 321-324 | 4 | 1 |
| α-helix | 334-338 | 5 | |
| β-strand | 343-346 | 4 | 1 |
| α-helix | 348-356 | 9 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-372 | 5 | 1 |
| α-helix | 374-376 | 3 | |
| α-helix | 382-394 | 13 | |
| α-helix | 403 | 1 | |
| β-strand | 404-408 | 5 | 1 |
| α-helix | 420-433 | 14 | |
| β-strand | 438 | 1 | 1 |
| α-helix | 446-449 | 4 | |
| β-strand | 457-462 | 6 | 2 |
| α-helix | 464-466 | 3 | |
| α-helix | 470-490 | 21 | |
| α-helix | 493-495 | 3 | |
| α-helix | 507-521 | 15 | |
| α-helix | 528-557 | 30 | |
| α-helix | 560-577 | 18 | |
| α-helix | 581-601 | 21 | |
| α-helix | 609-624 | 16 | |
| β-strand | 630 | 1 | 2 |
| β-strand | 633 | 1 | 2 |
| α-helix | 637-648 | 12 | |
| β-strand | 658-661 | 4 | 2 |
| α-helix | 675-684 | 10 | |
| β-strand | 693-696 | 4 | 2 |
| α-helix | 707-709 | 3 | |
| β-strand | 711 | 1 | 2 |
| β-strand | 714-715 | 2 | 2 |
| α-helix | 721-728 | 8 | |
| β-strand | 737-742 | 6 | 2 |
| α-helix | 747-768 | 22 | |
| α-helix | 773-791 | 19 | |
| α-helix | 800-802 | 3 | |
| β-strand | 806-810 | 5 | 3 |
| β-strand | 816-819 | 4 | 3 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-825 | 3 | 4 |
| β-strand | 832-833 | 2 | 4 |
| β-strand | 842-844 | 3 | 4 |
| β-strand | 861-864 | 4 | 4 |
| β-strand | 872-876 | 5 | 4 |
| β-strand | 885-887 | 3 | 4 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-896 | 5 | 3 |
| β-strand | 916-917 | 2 | 4 |
| α-helix | 918 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antiviral innate immune response receptor RIG-I | A | protein | 925 | Homo sapiens | O95786 (AlphaFold model) |
| OHSLR30 | B | RNA | 64 | Homo sapiens |
>8DVU_1 Antiviral innate immune response receptor RIG-I (chains A) MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKF LLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIP TDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERN KFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSP FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQI PVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTI PSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNT DEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMR DTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFL YTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESV SRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGI LTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGN VIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKI LHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKE CFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATG VQTLYSKWKDFHFEKIPFDPAEMSK
>8DVU_2 OHSLR30 (chains B) GGAUCGAUCGAUCGAUCGGCAUCGAUCGGCUUCGGCCGAUCGAUGCCGAUCGAUCGAUCG AUCC
The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands. Wang, W., Pyle, A.M. Mol Cell (2022) 82:4131-4144.e6. DOI 10.1016/j.molcel.2022.09.029 · PubMed
Other PDB entries of the same protein (UniProt O95786 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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