Structure of a classical MHC class I molecule that binds "non-classical" ligands.

Chicken YF1 genes share a close sequence relationship with classical MHC class I loci but map outside of the core MHC region. To obtain insights into their function, we determined the structure of the YF1*7.1/β(2)-microgloblin complex by X-ray crystallography at 1.3 Å resolution. It exhibits the arc...

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Autores principales:	Chee Seng Hee, Song Gao, Bernhard Loll, Marcia M Miller, Barbara Uchanska-Ziegler, Oliver Daumke, Andreas Ziegler
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/ea42851850d74fed891887ff1148576b
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spelling	oai:doaj.org-article:ea42851850d74fed891887ff1148576b2021-11-18T05:36:25ZStructure of a classical MHC class I molecule that binds "non-classical" ligands.1544-91731545-788510.1371/journal.pbio.1000557https://doaj.org/article/ea42851850d74fed891887ff1148576b2010-12-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21151886/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Chicken YF1 genes share a close sequence relationship with classical MHC class I loci but map outside of the core MHC region. To obtain insights into their function, we determined the structure of the YF17.1/β(2)-microgloblin complex by X-ray crystallography at 1.3 Å resolution. It exhibits the architecture typical of classical MHC class I molecules but possesses a hydrophobic binding groove that contains a non-peptidic ligand. This finding prompted us to reconstitute YF17.1 also with various self-lipids. Seven additional YF17.1 structures were solved, but only polyethyleneglycol molecules could be modeled into the electron density within the binding groove. However, an assessment of YF17.1 by native isoelectric focusing indicated that the molecules were also able to bind nonself-lipids. The ability of YF1*7.1 to interact with hydrophobic ligands is unprecedented among classical MHC class I proteins and might aid the chicken immune system to recognize a diverse ligand repertoire with a minimal number of MHC class I molecules.Chee Seng HeeSong GaoBernhard LollMarcia M MillerBarbara Uchanska-ZieglerOliver DaumkeAndreas ZieglerPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 8, Iss 12, p e1000557 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Chee Seng Hee Song Gao Bernhard Loll Marcia M Miller Barbara Uchanska-Ziegler Oliver Daumke Andreas Ziegler Structure of a classical MHC class I molecule that binds "non-classical" ligands.
description	Chicken YF1 genes share a close sequence relationship with classical MHC class I loci but map outside of the core MHC region. To obtain insights into their function, we determined the structure of the YF17.1/β(2)-microgloblin complex by X-ray crystallography at 1.3 Å resolution. It exhibits the architecture typical of classical MHC class I molecules but possesses a hydrophobic binding groove that contains a non-peptidic ligand. This finding prompted us to reconstitute YF17.1 also with various self-lipids. Seven additional YF17.1 structures were solved, but only polyethyleneglycol molecules could be modeled into the electron density within the binding groove. However, an assessment of YF17.1 by native isoelectric focusing indicated that the molecules were also able to bind nonself-lipids. The ability of YF1*7.1 to interact with hydrophobic ligands is unprecedented among classical MHC class I proteins and might aid the chicken immune system to recognize a diverse ligand repertoire with a minimal number of MHC class I molecules.
format	article
author	Chee Seng Hee Song Gao Bernhard Loll Marcia M Miller Barbara Uchanska-Ziegler Oliver Daumke Andreas Ziegler
author_facet	Chee Seng Hee Song Gao Bernhard Loll Marcia M Miller Barbara Uchanska-Ziegler Oliver Daumke Andreas Ziegler
author_sort	Chee Seng Hee
title	Structure of a classical MHC class I molecule that binds "non-classical" ligands.
title_short	Structure of a classical MHC class I molecule that binds "non-classical" ligands.
title_full	Structure of a classical MHC class I molecule that binds "non-classical" ligands.
title_fullStr	Structure of a classical MHC class I molecule that binds "non-classical" ligands.
title_full_unstemmed	Structure of a classical MHC class I molecule that binds "non-classical" ligands.
title_sort	structure of a classical mhc class i molecule that binds "non-classical" ligands.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/ea42851850d74fed891887ff1148576b
work_keys_str_mv	AT cheesenghee structureofaclassicalmhcclassimoleculethatbindsnonclassicalligands AT songgao structureofaclassicalmhcclassimoleculethatbindsnonclassicalligands AT bernhardloll structureofaclassicalmhcclassimoleculethatbindsnonclassicalligands AT marciammiller structureofaclassicalmhcclassimoleculethatbindsnonclassicalligands AT barbarauchanskaziegler structureofaclassicalmhcclassimoleculethatbindsnonclassicalligands AT oliverdaumke structureofaclassicalmhcclassimoleculethatbindsnonclassicalligands AT andreasziegler structureofaclassicalmhcclassimoleculethatbindsnonclassicalligands
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Structure of a classical MHC class I molecule that binds "non-classical" ligands.

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