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Structure of a Classical MHC Class I Molecule That Binds “Non-Classical” Ligands
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Structure of a Classical MHC Class I Molecule That Binds “Non-Classical” Ligands
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Journal Article
Structure of a Classical MHC Class I Molecule That Binds “Non-Classical” Ligands
2010
Overview
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 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.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ beta 2-Microglobulin - chemistry
/ beta 2-Microglobulin - metabolism
/ Histocompatibility Antigens Class I - chemistry
/ Histocompatibility Antigens Class I - immunology
/ Histocompatibility Antigens Class I - isolation & purification
/ Histocompatibility Antigens Class I - metabolism
/ Hydrophobic and Hydrophilic Interactions
/ Immunology/Antigen Processing and Recognition
/ Ligands
/ Lipids
/ Major histocompatibility complex
/ Poultry
/ Proteins
