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3bhb
From Proteopedia
| 3bhb, resolution 2.20Å () | |||||||||
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| Ligands: | |||||||||
| Non-Standard Residues: | |||||||||
| Gene: | HLA-A, HLAA (Homo sapiens), B2M (Homo sapiens) | ||||||||
| Domains: | IGc, MHC_I | ||||||||
| Related: | 3bgm, 3bh8, 3bh9, 3bha | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal Structure of KMD Phosphopeptide Bound to Human Class I MHC HLA-A2
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.
Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self., Mohammed F, Cobbold M, Zarling AL, Salim M, Barrett-Wilt GA, Shabanowitz J, Hunt DF, Engelhard VH, Willcox BE, Nat Immunol. 2008 Nov;9(11):1236-43. Epub 2008 Oct 5. PMID:18836451
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
3BHB is a 3 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Mohammed F, Cobbold M, Zarling AL, Salim M, Barrett-Wilt GA, Shabanowitz J, Hunt DF, Engelhard VH, Willcox BE. Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self. Nat Immunol. 2008 Nov;9(11):1236-43. Epub 2008 Oct 5. PMID:18836451 doi:10.1038/ni.1660
Page seeded by OCA on Tue Feb 17 01:00:30 2009
Categories: Homo sapiens | Barrett-Wilt, G A. | Cobbold, M. | Engelhard, V H. | Hunt, D F. | Mohammed, F. | Salim, M. | Shabanowitz, J. | Willcox, B E. | Zarling, A L. | Anchor residue | Glycoprotein | Hla-a2 | Host-virus interaction | Immune response | Immune system | Immunoglobulin domain | Mhc | Mhc i | Phosphopeptide | Phosphoprotein | Phosphoserine | Polymorphism | Transmembrane | Tumor antigen | Ubl conjugation
