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. Author manuscript; available in PMC: 2017 Jun 28.
Published in final edited form as: J Mol Biol. 2010 Mar 31;398(5):730ā€“746. doi: 10.1016/j.jmb.2010.03.047

Fig. 6.

Fig. 6

Distinct modes of peptide binding for Tiam1 and Syntenin PDZ domains. (a) The amino acid alignment of Syndecan-binding PDZ domains. Black and gray shading indicate that the residue is identical with or similar to that found in the Tiam1 PDZ domain, respectively. The pound sign (#) above the amino acid sequence indicates residues that participate in Tiam1 PDZ/ligand interactions. The gene accession codes are: Tiam1 (Q13009), Syntenin (O00560), Ca2+/calmodulin-associated Ser/Thr kinase (O14936), and GIPC (014908). (b) The binding surface and ligand-binding modes for the Tiam1 PDZ/Model and Syntenin PDZ2/Syndecan4 (PDB code 1OBY) complexes are compared. The three PDZ binding pockets (S0, Sāˆ’1 and Sāˆ’2) are highlighted in yellow and the orientation of each peptide is shown in stick representation. The Syntenin PDZ2/IL5RĪ± complex (PDB code 1OBX) illustrates how the C-terminal Phe residue of the peptide fits into the S0 pocket.