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It forms highly stable dimers and oligomers through its Leu\/Ile\/Phe\u2010rich domain, which is important for the stability and function of the protein. We recently resolved the partial 3D structure of this protein by NMR using a synthetic peptide encompassing amino acids Thr17 to Gln52, where the Leu\/Ile\/Phe\u2010 rich region was found to adopt a major alpha\u2010helix conformation spanning amino acids 23\u201339. Here, we report the resolution of the 3D structure of full\u2010length JCV agnoprotein by NMR, which not only confirmed the existence of the previously reported major \u03b1\u2010helix domain at the same position but also revealed the presence of an additional minor \u03b1\u2010helix region spanning amino acid residues Leu6 to lys13. The remaining regions of the protein adopt an intrinsically unstructured conformation. J. Cell. 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