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8D5F

The complex of Gtf2b neoantigen TGAARFDEF Presented by H2-Dd

Summary for 8D5F
Entry DOI10.2210/pdb8d5f/pdb
DescriptorH-2 class I histocompatibility antigen, D-D alpha chain, Beta-2-microglobulin, Transcription initiation factor IIB, ... (5 entities in total)
Functional Keywordscomplex, mhc, immune system
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains3
Total formula weight44774.12
Authors
Custodio, J.M.F.,Baker, B.M. (deposition date: 2022-06-04, release date: 2022-07-06, Last modification date: 2024-10-16)
Primary citationCustodio, J.M.,Ayres, C.M.,Rosales, T.J.,Brambley, C.A.,Arbuiso, A.G.,Landau, L.M.,Keller, G.L.J.,Srivastava, P.K.,Baker, B.M.
Structural and physical features that distinguish tumor-controlling from inactive cancer neoepitopes.
Proc.Natl.Acad.Sci.USA, 120:e2312057120-e2312057120, 2023
Cited by
PubMed Abstract: Neoepitopes arising from amino acid substitutions due to single nucleotide polymorphisms are targets of T cell immune responses to cancer and are of significant interest in the development of cancer vaccines. However, understanding the characteristics of rare protective neoepitopes that truly control tumor growth has been a challenge, due to their scarcity as well as the challenge of verifying true, neoepitope-dependent tumor control in humans. Taking advantage of recent work in mouse models that circumvented these challenges, here, we compared the structural and physical properties of neoepitopes that range from fully protective to immunologically inactive. As neoepitopes are derived from self-peptides that can induce immune tolerance, we studied not only how the various neoepitopes differ from each other but also from their wild-type counterparts. We identified multiple features associated with protection, including features that describe how neoepitopes differ from self as well as features associated with recognition by diverse T cell receptor repertoires. We demonstrate both the promise and limitations of neoepitope structural analysis and predictive modeling and illustrate important aspects that can be incorporated into neoepitope prediction pipelines.
PubMed: 38085776
DOI: 10.1073/pnas.2312057120
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.31 Å)
Structure validation

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