1ED3

CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.

Summary for 1ED3

• Entry DOI: 10.2210/pdb1ed3/pdb
• Descriptor: CLASS I MAJOR HISTOCOMPATIBILITY ANTIGEN RT1-AA, BETA-2-MICROGLOBULIN, PEPTIDE MTF-E (13N3E), ... (4 entities in total)
• Functional Keywords: major histocompatibility complex, rat minor histocompatibility complex, mhc, immunology, peptide antigen presentation, cellular immunity, cell surface receptor, t cell receptor ligand, immune system
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Membrane; Single-pass type I membrane protein: P16391; Secreted: P07151; Mitochondrion inner membrane; Multi-pass membrane protein: P05504
• Total number of polymer chains: 6
• Total formula weight: 90463.21

Authors

Speir, J.A.,Stevens, J.,Joly, E.,Butcher, G.W.,Wilson, I.A. (deposition date: 2000-01-26, release date: 2001-02-28, Last modification date: 2024-11-13)

Primary citation

Speir, J.A.,Stevens, J.,Joly, E.,Butcher, G.W.,Wilson, I.A.
Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa.
Immunity, 14:81-92, 2001

PubMed Abstract: The rat MHC class Ia molecule RT1-Aa has the unusual capacity to bind long peptides ending in arginine, such as MTF-E, a thirteen-residue, maternally transmitted minor histocompatibility antigen. The antigenic structure of MTF-E was unpredictable due to its extraordinary length and two arginines that could serve as potential anchor residues. The crystal structure of RT1-Aa-MTF-E at 2.55 A shows that both peptide termini are anchored, as in other class I molecules, but the central residues in two independent pMHC complexes adopt completely different bulged conformations based on local environment. The MTF-E epitope is fully exposed within the putative T cell receptor (TCR) footprint. The flexibility demonstrated by the MTF-E structures illustrates how different TCRs may be raised against chemically identical, but structurally dissimilar, pMHC complexes.

PubMed: 11163232
DOI: 10.1016/S1074-7613(01)00091-7

Experimental method

X-RAY DIFFRACTION (2.55 Å)