Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction

NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 Å fused with an maltose-binding protein (MB...

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Autores principales: Jin, Tengchuan, Huang, Mo, Jiang, Jiansheng, Smith, Patrick, Xiao, Tsan Sam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2018
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749810/
https://www.ncbi.nlm.nih.gov/pubmed/29293680
http://dx.doi.org/10.1371/journal.pone.0190547
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author Jin, Tengchuan
Huang, Mo
Jiang, Jiansheng
Smith, Patrick
Xiao, Tsan Sam
author_facet Jin, Tengchuan
Huang, Mo
Jiang, Jiansheng
Smith, Patrick
Xiao, Tsan Sam
author_sort Jin, Tengchuan
collection PubMed
description NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 Å fused with an maltose-binding protein (MBP) tag. Interestingly, the PYD domain forms a dimeric configuration through a disulfide bond in the crystal. The possible biological significance is discussed in the context of ROS induced NF-κB activation.
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spelling pubmed-57498102018-01-26 Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction Jin, Tengchuan Huang, Mo Jiang, Jiansheng Smith, Patrick Xiao, Tsan Sam PLoS One Research Article NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 Å fused with an maltose-binding protein (MBP) tag. Interestingly, the PYD domain forms a dimeric configuration through a disulfide bond in the crystal. The possible biological significance is discussed in the context of ROS induced NF-κB activation. Public Library of Science 2018-01-02 /pmc/articles/PMC5749810/ /pubmed/29293680 http://dx.doi.org/10.1371/journal.pone.0190547 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 (https://creativecommons.org/publicdomain/zero/1.0/) public domain dedication.
spellingShingle Research Article
Jin, Tengchuan
Huang, Mo
Jiang, Jiansheng
Smith, Patrick
Xiao, Tsan Sam
Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction
title Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction
title_full Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction
title_fullStr Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction
title_full_unstemmed Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction
title_short Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction
title_sort crystal structure of human nlrp12 pyd domain and implication in homotypic interaction
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749810/
https://www.ncbi.nlm.nih.gov/pubmed/29293680
http://dx.doi.org/10.1371/journal.pone.0190547
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