Q92752: Tenascin-R (TNR)

Tenascin-R (TNR) is a 1358-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92752.

Gene
TNR
Organism
Homo sapiens
Length
1358 residues
Mean pLDDT
78.5
Model
AF-Q92752-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.5 (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 accurate24%
70 to 90Confident: backbone generally right57%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and…

Subunit structure

Forms oligomers. Interacts with CNTN1, TNC, and FN1. Interacts with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B, PTPRZ1, and CSPG3 (By similarity)

Subcellular location

Secreted, extracellular space, extracellular matrix

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8FNAX-ray1.75 ÅA=1129-1358
8FN9X-ray1.8 ÅA/C/E/G=1129-1358

More AlphaFold highlights

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