Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction

Leucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Here authors solve the crystal structure of LRRTM2 in complex with its ligand Nrxn1β and shed light on how selective binding of ligands to LRRTM1/2 is achieved.

Bibliographic Details
Main Authors: Atsushi Yamagata, Sakurako Goto-Ito, Yusuke Sato, Tomoko Shiroshima, Asami Maeda, Masahiko Watanabe, Takashi Saitoh, Katsumi Maenaka, Tohru Terada, Tomoyuki Yoshida, Takeshi Uemura, Shuya Fukai
Format: Article
Language:English
Published: Nature Portfolio 2018-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-06333-8
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author Atsushi Yamagata
Sakurako Goto-Ito
Yusuke Sato
Tomoko Shiroshima
Asami Maeda
Masahiko Watanabe
Takashi Saitoh
Katsumi Maenaka
Tohru Terada
Tomoyuki Yoshida
Takeshi Uemura
Shuya Fukai
author_facet Atsushi Yamagata
Sakurako Goto-Ito
Yusuke Sato
Tomoko Shiroshima
Asami Maeda
Masahiko Watanabe
Takashi Saitoh
Katsumi Maenaka
Tohru Terada
Tomoyuki Yoshida
Takeshi Uemura
Shuya Fukai
author_sort Atsushi Yamagata
collection DOAJ
description Leucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Here authors solve the crystal structure of LRRTM2 in complex with its ligand Nrxn1β and shed light on how selective binding of ligands to LRRTM1/2 is achieved.
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spelling doaj.art-6a3dc0e46ef84edea9ccf79ebc62bca02022-12-21T19:26:40ZengNature PortfolioNature Communications2041-17232018-09-019111110.1038/s41467-018-06333-8Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interactionAtsushi Yamagata0Sakurako Goto-Ito1Yusuke Sato2Tomoko Shiroshima3Asami Maeda4Masahiko Watanabe5Takashi Saitoh6Katsumi Maenaka7Tohru Terada8Tomoyuki Yoshida9Takeshi Uemura10Shuya Fukai11Institute for Quantitative Biosciences, The University of TokyoInstitute for Quantitative Biosciences, The University of TokyoInstitute for Quantitative Biosciences, The University of TokyoInstitute for Quantitative Biosciences, The University of TokyoInstitute for Quantitative Biosciences, The University of TokyoDepartment of Anatomy, Hokkaido University Faculty of MedicineDepartment of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University of ScienceCenter for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido UniversityInterfaculty Initiative in Information Studies, The University of TokyoDepartment of Molecular Neuroscience, Graduate School of Medicine and Pharmaceutical Sciences, University of ToyamaCREST, JSTInstitute for Quantitative Biosciences, The University of TokyoLeucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Here authors solve the crystal structure of LRRTM2 in complex with its ligand Nrxn1β and shed light on how selective binding of ligands to LRRTM1/2 is achieved.https://doi.org/10.1038/s41467-018-06333-8
spellingShingle Atsushi Yamagata
Sakurako Goto-Ito
Yusuke Sato
Tomoko Shiroshima
Asami Maeda
Masahiko Watanabe
Takashi Saitoh
Katsumi Maenaka
Tohru Terada
Tomoyuki Yoshida
Takeshi Uemura
Shuya Fukai
Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
Nature Communications
title Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
title_full Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
title_fullStr Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
title_full_unstemmed Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
title_short Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
title_sort structural insights into modulation and selectivity of transsynaptic neurexin lrrtm interaction
url https://doi.org/10.1038/s41467-018-06333-8
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