3BH9
Crystal Structure of RTY Phosphopeptide Bound to Human Class I MHC HLA-A2
Summary for 3BH9
| Entry DOI | 10.2210/pdb3bh9/pdb |
| Related | 3BGM 3BH8 3BHA 3BHB |
| Descriptor | HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, decameric peptide from Protein POF1B, ... (6 entities in total) |
| Functional Keywords | phosphoserine, phosphopeptide, mhc, hla-a2, anchor residue, tumor antigen, glycoprotein, host-virus interaction, immune response, mhc i, polymorphism, transmembrane, ubl conjugation, immunoglobulin domain, phosphoprotein, immune system |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Membrane; Single-pass type I membrane protein: P01892 Secreted . Note=(Microbial infection) In the presence of M: P61769 Cell junction, tight junction : Q8WVV4 |
| Total number of polymer chains | 3 |
| Total formula weight | 45115.00 |
| Authors | Mohammed, F.,Cobbold, M.,Zarling, A.L.,Salim, M.,Barrett-Wilt, G.A.,Shabanowitz, J.,Hunt, D.F.,Engelhard, V.H.,Willcox, B.E. (deposition date: 2007-11-28, release date: 2008-10-21, Last modification date: 2024-10-30) |
| Primary citation | Mohammed, F.,Cobbold, M.,Zarling, A.L.,Salim, M.,Barrett-Wilt, G.A.,Shabanowitz, J.,Hunt, D.F.,Engelhard, V.H.,Willcox, B.E. Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self Nat.Immunol., 9:1236-1243, 2008 Cited by PubMed Abstract: Protein phosphorylation generates a source of phosphopeptides that are presented by major histocompatibility complex class I molecules and recognized by T cells. As deregulated phosphorylation is a hallmark of malignant transformation, the differential display of phosphopeptides on cancer cells provides an immunological signature of 'transformed self'. Here we demonstrate that phosphorylation can considerably increase peptide binding affinity for HLA-A2. To understand this, we solved crystal structures of four phosphopeptide-HLA-A2 complexes. These identified a novel peptide-binding motif centered on a solvent-exposed phosphate anchor. Our findings indicate that deregulated phosphorylation can create neoantigens by promoting binding to major histocompatibility complex molecules or by affecting the antigenic identity of presented epitopes. These results highlight the potential of phosphopeptides as novel targets for cancer immunotherapy. PubMed: 18836451DOI: 10.1038/ni.1660 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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