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.

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Autores principales: 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
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/6a3dc0e46ef84edea9ccf79ebc62bca0
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spelling oai:doaj.org-article:6a3dc0e46ef84edea9ccf79ebc62bca02021-12-02T16:49:34ZStructural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction10.1038/s41467-018-06333-82041-1723https://doaj.org/article/6a3dc0e46ef84edea9ccf79ebc62bca02018-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06333-8https://doaj.org/toc/2041-1723Leucine-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.Atsushi YamagataSakurako Goto-ItoYusuke SatoTomoko ShiroshimaAsami MaedaMasahiko WatanabeTakashi SaitohKatsumi MaenakaTohru TeradaTomoyuki YoshidaTakeshi UemuraShuya FukaiNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
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.
format article
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
title 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_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_sort structural insights into modulation and selectivity of transsynaptic neurexin–lrrtm interaction
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/6a3dc0e46ef84edea9ccf79ebc62bca0
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