P61372: Insulin gene enhancer protein ISL-1 (Isl1)

Insulin gene enhancer protein ISL-1 (Isl1) is a 349-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61372.

Gene
Isl1
Organism
Mus musculus
Length
349 residues
Mean pLDDT
71.0
Model
AF-P61372-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.0 (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 accurate32%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

DNA-binding transcriptional activator (PubMed:14664703, PubMed:18539116, PubMed:22343712, PubMed:24643061, PubMed:25775587). Recognizes and binds to the consensus octamer binding site 5'-ATAATTAA-3' in promoter of target genes (PubMed:18539116, PubMed:24643061, PubMed:25775587). Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation (PubMed:25775587). Cooperates with the transcription factor POU4F2 to achieve maximal levels of expression of RGC target genes and RGC fate specification in the developing retina (PubMed:24643061, PubMed:25775587). Involved in the specification of motor neurons in cooperation with LHX3 and LDB1…

Subunit structure

At neuronal promoters, displaces LDB1 from LHX3 LIM domain to form a ternary complex in which ISL1 contacts both LHX3 and LDB1; allosteric structural changes in the DNA binding domain of LHX3, induced by the ISL1:LHX3 interaction, may explain differences in sequence specificity of the different complexes (PubMed:18539116, PubMed:18583962). Interacts with LHX3 (PubMed:18539116). Interacts (via…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2RGTX-ray2.05 ÅA/B=139-168
4JCJX-ray3.0 ÅA/B/C=11-138

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