Q99836: Myeloid differentiation primary response protein MyD88 (MYD88)

Myeloid differentiation primary response protein MyD88 (MYD88) is a 296-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99836.

Gene
MYD88
Organism
Homo sapiens
Length
296 residues
Mean pLDDT
80.6
Model
AF-Q99836-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.6 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate15%
70 to 90Confident: backbone generally right69%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response (PubMed:15361868, PubMed:18292575, PubMed:33718825, PubMed:37971847). Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:15361868, PubMed:19506249, PubMed:24316379, PubMed:40638072). Increases IL-8 transcription (PubMed:9013863). Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses…

Subunit structure

Homodimer. Also forms heterodimers with TIRAP (PubMed:17322885, PubMed:19506249, PubMed:19948740). Binds to TLR2, TLR5, IRAK1, IRAK2 and IRAK4 via their respective TIR domains. Interacts with IL18R1. Interacts with BMX, IL1RL1, IKBKE and IRF7. Interacts with LRRFIP1 and LRRFIP2; this interaction positively regulates Toll-like receptor (TLR) signaling in response to agonist. Interacts with FLII.…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
4EO7X-ray1.45 ÅA=157-296
9HFVX-ray1.45 ÅB=127-146
4DOMX-ray1.8 ÅA=157-296
9HGHX-ray1.9 ÅB=125-141
7BERX-ray2.3 ÅA=155-296
7L6WX-ray2.3 ÅA=159-296
8S78EM2.85 ÅA=154-296
7BEQEM3.0 ÅA=155-296
6I3NEM3.1 ÅA/B/C/D/E/F/G/H/I/J/K/L/M=1-151
8W8MEM3.28 Å1A/1B/1C/1D/1E/1F/2A/2B/2C/2D/2E/2F/3A/3B/3C/3D/3E/3F/A1/A2/A3/B1/B2/B3/C1/C2/C3/D1/D2/D3=153-296
8YYMEM3.3 ÅA/AA/AB/AC/B/BA/BB/BC/C/CA/CB/CC/D/DA/DB/DC/E/EA/EB/EC/F/FA/FB/FC/G/GA/GB/GC/H/HA=153-296
3MOPX-ray3.4 ÅA/B/C/D/E/F=20-117
2JS7NMRA=146-296
2Z5VNMRA=148-296

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