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

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Official URL:https://doi.org/10.1371/journal.pbio.1000557
PubMed:View item in PubMed
Creators Name:Hee, C.S. and Gao, S. and Loll, B. and Miller, M.M. and Uchanska-Ziegler, B. and Daumke, O. and Ziegler, A.
Journal Title:PLoS Biology
Journal Abbreviation:PLoS Biol
Volume:8
Number:12
Page Range:e1000557
Date:7 December 2010
Keywords:beta 2-Microglobulin, Histocompatibility Antigens Class I Purification, Hydrophobic and Hydrophilic Interactions, Isoelectric Focusing, MHC Class I Genes, X-Ray Crystallography, Animals, Chickens
Abstract: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/beta(2)-microgloblin complex by X-ray crystallography at 1.3 A 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 YF1*7.1 also with various self-lipids. Seven additional YF1*7.1 structures were solved, but only polyethyleneglycol molecules could be modeled into the electron density within the binding groove. However, an assessment of YF1*7.1 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.
ISSN:1544-9173
Publisher:Public Library of Science (U.S.A.)
Item Type:Article

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