3O3A

Human Class I MHC HLA-A2 in complex with the Peptidomimetic ELA-1

Summary for 3O3A

• Entry DOI: 10.2210/pdb3o3a/pdb
• Related: 2GT9 3O3B 3O3D 3O3E
• Descriptor: HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, Peptidomimetic ELA-1, ... (5 entities in total)
• Functional Keywords: mart peptides, nonapeptide, mhc class i, hla-a2, peptidomimetics, cross-reactivity, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted: P61769
• Total number of polymer chains: 6
• Total formula weight: 90250.28

Authors

Borbulevych, O.Y.,Baker, B.M. (deposition date: 2010-07-23, release date: 2010-12-08, Last modification date: 2024-11-06)

Primary citation

Douat-Casassus, C.,Borbulevych, O.,Tarbe, M.,Gervois, N.,Jotereau, F.,Baker, B.M.,Quideau, S.
Crystal structures of HLA-A*0201 complexed with Melan-A/MART-1(26(27L)-35) peptidomimetics reveal conformational heterogeneity and highlight degeneracy of T cell recognition.
J.Med.Chem., 53:7061-7066, 2010

PubMed Abstract: There is growing interest in using tumor associated antigens presented by class I major histocompatibility complex (MHC-I) proteins as cancer vaccines. As native peptides are poorly stable in biological fluids, researchers have sought to engineer synthetic peptidomimetics with greater biostability. Here, we demonstrate that antigenic peptidomimetics of the Melan-A/MART-1(26(27L)-35) melanoma antigen adopt strikingly different conformations when bound to MHC-I, highlighting the degeneracy of T cell recognition and revealing the challenges associated with mimicking native peptide conformation.

PubMed: 20806940
DOI: 10.1021/jm100683p

Experimental method

X-RAY DIFFRACTION (1.8 Å)