Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered

Even though the human genome project showed that our DNA contains a mere 20,000 to 25,000 protein coding genes, an unexpectedly large number of these proteins remain functionally uncharacterized. A structural characterization of these unknown proteins may help to identify possible cellular tasks. We therefore used a combination of bioinformatics and nuclear magnetic resonance spectroscopy to structurally de-orphanize one of these gene products, the 108 amino acid human uncharacterized protein CXorf51A. Both our bioinformatics analysis as well as the H-1, C-13, N-15 backbone and near-complete side-chain chemical shift assignments indicate that it is an intrinsically disordered protein.

Automated summary

The Human Genome Project revealed that the human DNA contains 20,000 to 25,000 protein coding genes, with a large number of these proteins remaining functionally uncharacterized. Structural characterization of these unknown proteins may help identify their cellular tasks. By using bioinformatics and nuclear magnetic resonance spectroscopy, researchers were able to determine that the 108 amino acid human uncharacterized protein CXorf51A is an intrinsically disordered protein.