Fig. 3: TEN2 and LPHN3 interaction is mediated by conserved residues. | Nature Communications

Fig. 3: TEN2 and LPHN3 interaction is mediated by conserved residues.

From: Alternative splicing controls teneurin-latrophilin interaction and synapse specificity by a shape-shifting mechanism

Fig. 3

a The TEN2/LPHN3 binding interface is conserved. The structure of the TEN2/LPHN3 complex is shown in surface representation on which the conservation of residues is mapped from most conserved (magenta) to least conserved (cyan) (using the ConSurf server63). The LPHN-binding site on TEN2 and the TEN2-binding site on LPHN3 are indicated by yellow circles. b Ribbon diagram of the TEN2/LPHN3 heterodimer showing the interface between TEN2 and LPHN3. Close-up view of the binding interface shows tentative residues involved hydrogen bonds and salt bridge shown by yellow dashes and red dashes, respectively. The TEN2 mutation DHR mutation (D1737N, H1738T, R1739T) which disrupt the TEN2/LPHN3 are shown as sticks. Two salt bridges between R44 and E2001; two between D49 and R2043; one between D49 and R2043; and one between D67 and K1712 are observed. c Close-up view for the EM density showing the close packing of the conserved N-linked glycosylation on TEN2-N1681 with LPHN3-S38 on the Lec domain. Due to the uncertainty of the glycan topology, we only modeled the first three sugars of N-glycosylation (NAG-NAG-BMA) into the density.

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