Fig. 1
From: Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation
Overall structures of the 2:2 heterotetrameric SALM5/PTPδ complex, SALM5 dimer, and monomer. a Domain organization of human SALM5 and human PTPδ. LRR: leucine-rich repeats domain; Ig: Ig-like domain; Fn: fibronectin type III domain; D1, D2: a tandem of tyrosine–protein phosphatase domains; Me: mini exon; TM: transmembrane domain; N: N-terminus; C: C-terminus. b Surface representation of the dimeric SALM5/PTPδ complex. The LRR domain and Ig domain in SALM5 are colored cyan and yellow, respectively. The Ig1, Ig2, and Ig3 domains in PTPδ are colored magenta, green, and orange, respectively. c Top view of the dimeric SALM5/PTPδ complex shown in ribbons. d Side view of the SALM5 dimer (extracted from PTPδ-bound complex structure) in ribbons. e Ribbon representation of SALM5 LRR-Ig domains. Disulfide bonds are indicated using yellow sticks. Color codes are as follows: LRRNT, pink; LRRs 1–7, cyan; LRRNT, slate; R-loop, green; Ig domain, orange. c, d The N-linked glycans are indicated as sticks, and three glycosylation sites (N73, N330, and N339) of one SALM5 molecule are labeled. The N and C terminus of each molecule are, respectively, labeled as “N-ter” and “C-ter”
