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. 1997 Dec 9;94(25):13683–13688. doi: 10.1073/pnas.94.25.13683

Figure 5.

Figure 5

Sequence alignment of selected PDZ domains. The first (SYNT PDZ-1) and second (SYNT PDZ-2) PDZ domains of syntenin were aligned to the three PDZ domains of the rat brain postsynaptic density protein PSD-95 (M96853), PDZ-3 of the Drosophila Discs-large or Dlg protein (M73529), and its human homolog hDlg (U49089); PDZ-2 of the human tight junction protein ZO-1 (L14837); PDZ-3 of human ZO-2 (L27152), the PDZ domain of rat neuronal nitric oxide synthase or nNOS (X59949); the PDZ domain of murine Tiam-1 (U05245); the PDZ domain of the Caenorhabditis elegans protein LIN-2a (X92564); and the PDZ domain of the human p55 erythrocyte membrane protein (M64925). The numbers in parenthesis refer to the GenBank database accession numbers for the nucleotide sequences that encode these proteins. The residues forming the hydrophobic pockets are indicated by asterisks. The conserved basic residues in the carboxylate binding (CB) loop, involved in the stabilization of the terminal carboxylate group, and the αB1 residues that select for the residues at the −2 positions of the peptide are indicated in bold and with a caret. For more details we refer to the papers of Doyle et al. (14) and Morais Cabral et al. (19).