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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2019
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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. |
format | Online Article Text |
id | pubmed-6450527 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
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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