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. Author manuscript; available in PMC: 2009 Jun 1.
Published in final edited form as: Mol Immunol. 2008 Apr 8;45(11):3244–3252. doi: 10.1016/j.molimm.2008.02.022

Figure 6. Proposed model of arginine residues in the C1q B chain globular domain interacting with fibrillar Aβ.

Figure 6

The C1q B chain model was generated directly from the coordinates of the crystal structure of C1q globular head (Gaboriaud et al., 2003). Only the arginine side chains (R101, R114, R129) of the C1q B-chain and the aspartic and glutamic acids of the amyloid peptide are shown as space filling models. One possible interaction with Asp7 and Glu11 of the Aβ fibril constrained in an antiparallel β-sheet conformation is illustrated.