3P73

Crystal Structures of the Chicken YF1*7.1 molecule

Summary for 3P73

• Entry DOI: 10.2210/pdb3p73/pdb
• Related: 3P77 3bev 3bew
• Descriptor: MHC Rfp-Y class I alpha chain, Beta-2-microglobulin, CETYL-TRIMETHYL-AMMONIUM, ... (5 entities in total)
• Functional Keywords: ig-like c1-type (immunoglobulin-like) domain, histocompatibility antigen, immune system
• Biological source: Gallus gallus (bantam,chickens); More
• Cellular location: Secreted: P21611
• Total number of polymer chains: 2
• Total formula weight: 43203.53

Authors

Hee, C.S.,Gao, S.,Loll, B.,Miller, M.M.,Uchanska-Ziegler, B.,Daumke, O.,Ziegler, A. (deposition date: 2010-10-12, release date: 2010-11-24, Last modification date: 2024-11-06)

Primary citation

Hee, C.S.,Gao, S.,Loll, B.,Miller, M.M.,Uchanska-Ziegler, B.,Daumke, O.,Ziegler, A.
Structure of a Classical MHC Class I Molecule That Binds "Non-Classical" Ligands.
Plos Biol., 8:e1000557-e1000557, 2010

PubMed 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/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.

PubMed: 21151886
DOI: 10.1371/journal.pbio.1000557

Experimental method

X-RAY DIFFRACTION (1.32 Å)