Ontology highlight
ABSTRACT:
SUBMITTER: Lin Z
PROVIDER: S-EPMC5773555 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Lin Zhaohan Z Liu Jianmei J Ding Huandi H Xu Fei F Liu Heli H
Nature communications 20180118 1
SALM5, a synaptic adhesion molecule implicated in autism, induces presynaptic differentiation through binding to the LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) that have been highlighted as presynaptic hubs for synapse formation. The mechanisms underlying SALM5/LAR-RPTP interaction remain unsolved. Here we report crystal structures of human SALM5 LRR-Ig alone and in complex with human PTPδ Ig1-3 (MeA<sup>-</sup>). Distinct from other LAR-RPTP ligands, SALM5 mainly exists as a ...[more]