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3P77

Crystal Structures of the Chicken YF1*7.1 molecule

Summary for 3P77
Entry DOI10.2210/pdb3p77/pdb
Related3P73 3bev 3bew
DescriptorMHC Rfp-Y class I alpha chain, Beta-2-microglobulin, ACETATE ION, ... (6 entities in total)
Functional Keywordsig-like c1-type (immunoglobulin-like) domain, histocompatibility antigen, immune system
Biological sourceGallus gallus (bantam,chickens)
More
Cellular locationSecreted: P21611
Total number of polymer chains2
Total formula weight43692.87
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: 2024-10-30)
Primary citationHee, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

227111

數據於2024-11-06公開中

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