Figure 2 | Scientific Reports

Figure 2

From: Tau Antibody Structure Reveals a Molecular Switch Defining a Pathological Conformation of the Tau Protein

Figure 2

Structure of the Fab C5.2 and pSer396/pSer404 Tau peptide. (a) A front view ribbon representation of Fab C5.2 in complex with a pS396/pS404 peptide. Although the peptide used in crystallization is 23 residues in length, only seven residues, containing Ser396 phosphorylation, were visible in the electron density map (392IVYKpSPV398). The side chain of pSer396 and an orphan phosphate are represented as ball and stick. The heavy and light chains are colored light green and cyan, respectively. (b) A side view of the Fab C5.2:peptide complex. (c) A top view of antigen-binding site annotated by CDR loops. CDR-1, -2, and -3 are colored in salmon, orange and yellow, respectively. (d) Molecular surface of the electrostatic potential of the C5.2 antigen-binding site, colored from negative (red) to positive (blue). Note the strong, complementary electropositive surface near the phosphate molecules.

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