Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility

The MILL (MHC-I-like located near the leukocyte receptor complex) family is a group of related nonclassical MHC-I molecules. Here the authors present the crystal structure of MILL2, which reveals an unusual interdomain flexibility, and show that MILL2 binds heparan sulfate on the surface of fibrobla...

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Autores principales:	Mizuho Kajikawa, Toyoyuki Ose, Yuko Fukunaga, Yuki Okabe, Naoki Matsumoto, Kento Yonezawa, Nobutaka Shimizu, Simon Kollnberger, Masanori Kasahara, Katsumi Maenaka
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3341d66dc08e4602846e819f01a70df7
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spelling	oai:doaj.org-article:3341d66dc08e4602846e819f01a70df72021-12-02T15:34:00ZStructure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility10.1038/s41467-018-06797-82041-1723https://doaj.org/article/3341d66dc08e4602846e819f01a70df72018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06797-8https://doaj.org/toc/2041-1723The MILL (MHC-I-like located near the leukocyte receptor complex) family is a group of related nonclassical MHC-I molecules. Here the authors present the crystal structure of MILL2, which reveals an unusual interdomain flexibility, and show that MILL2 binds heparan sulfate on the surface of fibroblasts through a basic patch.Mizuho KajikawaToyoyuki OseYuko FukunagaYuki OkabeNaoki MatsumotoKento YonezawaNobutaka ShimizuSimon KollnbergerMasanori KasaharaKatsumi MaenakaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Mizuho Kajikawa Toyoyuki Ose Yuko Fukunaga Yuki Okabe Naoki Matsumoto Kento Yonezawa Nobutaka Shimizu Simon Kollnberger Masanori Kasahara Katsumi Maenaka Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
description	The MILL (MHC-I-like located near the leukocyte receptor complex) family is a group of related nonclassical MHC-I molecules. Here the authors present the crystal structure of MILL2, which reveals an unusual interdomain flexibility, and show that MILL2 binds heparan sulfate on the surface of fibroblasts through a basic patch.
format	article
author	Mizuho Kajikawa Toyoyuki Ose Yuko Fukunaga Yuki Okabe Naoki Matsumoto Kento Yonezawa Nobutaka Shimizu Simon Kollnberger Masanori Kasahara Katsumi Maenaka
author_facet	Mizuho Kajikawa Toyoyuki Ose Yuko Fukunaga Yuki Okabe Naoki Matsumoto Kento Yonezawa Nobutaka Shimizu Simon Kollnberger Masanori Kasahara Katsumi Maenaka
author_sort	Mizuho Kajikawa
title	Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
title_short	Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
title_full	Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
title_fullStr	Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
title_full_unstemmed	Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
title_sort	structure of mhc class i-like mill2 reveals heparan-sulfate binding and interdomain flexibility
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/3341d66dc08e4602846e819f01a70df7
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Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility

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