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. 2009 Aug 7;284(41):28430–28441. doi: 10.1074/jbc.M109.031419

FIGURE 8.

FIGURE 8.

Mechanism of NEU1 oligomerization. A, each NEU1 monomer (red circles) has two binding sites on its surface (1 and 2). Monomers bind to each other and form a spiral chain that varies in length. PPCA homodimers (green spheres) compete for binding to NEU1-binding sites 1 or 2 at the ends of the NEU1 chain. B, this results in the formation of PPCA-NEU1 heterodimers and a shorter NEU1 oligomeric chain. C, a structural model of the NEU1 oligomer. Peptide 1 (cyan) of the first molecule interacts with peptide 2 (dark blue) of the second molecule. A free peptide 1 of the second molecule interacts with a free peptide 2 of the third molecule and so on. The distance between the tips of these peptides and the center of the molecule is 25–26 Å, and they are oriented at roughly 70° in relation to each other. D, electron micrograph of purified BV-NEU1 protein confirms the spiral chain structure of the NEU1 oligomers. Scale bar, 7 nm.