1ed3
From Proteopedia
|
CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.
Overview
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.
About this Structure
1ED3 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa., Speir JA, Stevens J, Joly E, Butcher GW, Wilson IA, Immunity. 2001 Jan;14(1):81-92. PMID:11163232
Page seeded by OCA on Tue Nov 20 13:54:27 2007
Categories: Protein complex | Rattus norvegicus | Butcher, G.W. | Joly, E. | Speir, J.A. | Stevens, J. | Wilson, I.A. | Cell surface receptor | Cellular immunity | Immunology | Major histocompatibility complex | Mhc | Peptide antigen presentation | Rat minor histocompatibility complex | T cell receptor ligand
