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Crystallization of the human tetraspanin protein CD9

The tetraspanin family of proteins with four membrane-spanning proteins function in a wide range of physiological processes in higher organisms, including cell migration and proliferation, cell fusion, fertilization and virus infection. Although the recently reported structure of CD81 unveiled the b...

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Detalles Bibliográficos
Autores principales: Umeda, Rie, Nishizawa, Tomohiro, Nureki, Osamu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6450527/
https://www.ncbi.nlm.nih.gov/pubmed/30950826
http://dx.doi.org/10.1107/S2053230X1801840X
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author Umeda, Rie
Nishizawa, Tomohiro
Nureki, Osamu
author_facet Umeda, Rie
Nishizawa, Tomohiro
Nureki, Osamu
author_sort Umeda, Rie
collection PubMed
description The tetraspanin family of proteins with four membrane-spanning proteins function in a wide range of physiological processes in higher organisms, including cell migration and proliferation, cell fusion, fertilization and virus infection. Although the recently reported structure of CD81 unveiled the basic architecture of this family for the first time, further structural and functional studies are required in order to understand the mechanistic details of the complicated functions of the tetraspanin-family proteins. In this study, attempts were made to crystallize human CD9, a representative member of the tetraspanin family, and it was demonstrated that the truncation of a variable region in the second long extracellular loop significantly improved crystal growth.
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spelling pubmed-64505272019-04-19 Crystallization of the human tetraspanin protein CD9 Umeda, Rie Nishizawa, Tomohiro Nureki, Osamu Acta Crystallogr F Struct Biol Commun Research Communications The tetraspanin family of proteins with four membrane-spanning proteins function in a wide range of physiological processes in higher organisms, including cell migration and proliferation, cell fusion, fertilization and virus infection. Although the recently reported structure of CD81 unveiled the basic architecture of this family for the first time, further structural and functional studies are required in order to understand the mechanistic details of the complicated functions of the tetraspanin-family proteins. In this study, attempts were made to crystallize human CD9, a representative member of the tetraspanin family, and it was demonstrated that the truncation of a variable region in the second long extracellular loop significantly improved crystal growth. International Union of Crystallography 2019-04-02 /pmc/articles/PMC6450527/ /pubmed/30950826 http://dx.doi.org/10.1107/S2053230X1801840X Text en © Umeda et al. 2019 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Communications
Umeda, Rie
Nishizawa, Tomohiro
Nureki, Osamu
Crystallization of the human tetraspanin protein CD9
title Crystallization of the human tetraspanin protein CD9
title_full Crystallization of the human tetraspanin protein CD9
title_fullStr Crystallization of the human tetraspanin protein CD9
title_full_unstemmed Crystallization of the human tetraspanin protein CD9
title_short Crystallization of the human tetraspanin protein CD9
title_sort crystallization of the human tetraspanin protein cd9
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6450527/
https://www.ncbi.nlm.nih.gov/pubmed/30950826
http://dx.doi.org/10.1107/S2053230X1801840X
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