Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding
Collagen lysyl hydroxylases promote cancer progression. Here the authors present the crystal structure of the lysyl hydroxylase domain of L230 from Acanthamoeba polyphaga mimivirus, which is of interest for LH inhibitor development, and show that ectopic expression of L230 in tumors promotes collage...
Guardado en:
Autores principales: | , , , , , , , , , , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/66b3577e6b604e7983c92825500bf879 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:66b3577e6b604e7983c92825500bf879 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:66b3577e6b604e7983c92825500bf8792021-12-02T14:40:08ZPro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding10.1038/s41467-018-02859-z2041-1723https://doaj.org/article/66b3577e6b604e7983c92825500bf8792018-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-02859-zhttps://doaj.org/toc/2041-1723Collagen lysyl hydroxylases promote cancer progression. Here the authors present the crystal structure of the lysyl hydroxylase domain of L230 from Acanthamoeba polyphaga mimivirus, which is of interest for LH inhibitor development, and show that ectopic expression of L230 in tumors promotes collagen cross-linking and metastasis.Hou-Fu GuoChi-Lin TsaiMasahiko TerajimaXiaochao TanPriyam BanerjeeMitchell D. MillerXin LiuJiang YuJovita ByemerwaSarah AlvaradoTamer S. KaoudKevin N. DalbyNeus Bota-RabassedasYulong ChenMitsuo YamauchiJohn A. TainerGeorge N. PhillipsJonathan M. KurieNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Science Q |
spellingShingle |
Science Q Hou-Fu Guo Chi-Lin Tsai Masahiko Terajima Xiaochao Tan Priyam Banerjee Mitchell D. Miller Xin Liu Jiang Yu Jovita Byemerwa Sarah Alvarado Tamer S. Kaoud Kevin N. Dalby Neus Bota-Rabassedas Yulong Chen Mitsuo Yamauchi John A. Tainer George N. Phillips Jonathan M. Kurie Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding |
description |
Collagen lysyl hydroxylases promote cancer progression. Here the authors present the crystal structure of the lysyl hydroxylase domain of L230 from Acanthamoeba polyphaga mimivirus, which is of interest for LH inhibitor development, and show that ectopic expression of L230 in tumors promotes collagen cross-linking and metastasis. |
format |
article |
author |
Hou-Fu Guo Chi-Lin Tsai Masahiko Terajima Xiaochao Tan Priyam Banerjee Mitchell D. Miller Xin Liu Jiang Yu Jovita Byemerwa Sarah Alvarado Tamer S. Kaoud Kevin N. Dalby Neus Bota-Rabassedas Yulong Chen Mitsuo Yamauchi John A. Tainer George N. Phillips Jonathan M. Kurie |
author_facet |
Hou-Fu Guo Chi-Lin Tsai Masahiko Terajima Xiaochao Tan Priyam Banerjee Mitchell D. Miller Xin Liu Jiang Yu Jovita Byemerwa Sarah Alvarado Tamer S. Kaoud Kevin N. Dalby Neus Bota-Rabassedas Yulong Chen Mitsuo Yamauchi John A. Tainer George N. Phillips Jonathan M. Kurie |
author_sort |
Hou-Fu Guo |
title |
Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding |
title_short |
Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding |
title_full |
Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding |
title_fullStr |
Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding |
title_full_unstemmed |
Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding |
title_sort |
pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by fe2+-binding |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/66b3577e6b604e7983c92825500bf879 |
work_keys_str_mv |
AT houfuguo prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT chilintsai prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT masahikoterajima prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT xiaochaotan prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT priyambanerjee prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT mitchelldmiller prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT xinliu prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT jiangyu prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT jovitabyemerwa prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT sarahalvarado prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT tamerskaoud prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT kevinndalby prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT neusbotarabassedas prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT yulongchen prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT mitsuoyamauchi prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT johnatainer prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT georgenphillips prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding AT jonathanmkurie prometastaticcollagenlysylhydroxylasedimerassembliesstabilizedbyfe2binding |
_version_ |
1718390417758617600 |