4PG9

MHC Class I in complex with Sendai virus nucleoprotein peptide FAPGNYPAL

Summary for 4PG9

• Entry DOI: 10.2210/pdb4pg9/pdb
• Related: 4PGB 4PGC 4PGD 4PGE
• Descriptor: H-2 class I histocompatibility antigen, K-B alpha chain, Beta-2-microglobulin, Sendai virus nucleoprotein, ... (5 entities in total)
• Functional Keywords: immune system, immunoglobulin domain, immune response, immune system-peptide complex, immune system/peptide
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 3
• Total formula weight: 48662.55

Authors

Celie, P.,Joosten, R.P.,Perrakis, A.,Neefjes, J. (deposition date: 2014-05-01, release date: 2015-01-07, Last modification date: 2024-10-23)

Primary citation

Garstka, M.A.,Fish, A.,Celie, P.H.,Joosten, R.P.,Janssen, G.M.,Berlin, I.,Hoppes, R.,Stadnik, M.,Janssen, L.,Ovaa, H.,van Veelen, P.A.,Perrakis, A.,Neefjes, J.
The first step of peptide selection in antigen presentation by MHC class I molecules.
Proc.Natl.Acad.Sci.USA, 112:1505-1510, 2015

PubMed Abstract: MHC class I molecules present a variable but limited repertoire of antigenic peptides for T-cell recognition. Understanding how peptide selection is achieved requires mechanistic insights into the interactions between the MHC I and candidate peptides. We find that, at first encounter, MHC I H-2K(b) considers a wide range of peptides, including those with expanded N termini and unfitting anchor residues. Discrimination occurs in the second step, when noncanonical peptides dissociate with faster exchange rates. This second step exhibits remarkable temperature sensitivity, as illustrated by numerous noncanonical peptides presented by H-2K(b) in cells cultured at 26 °C relative to 37 °C. Crystallographic analyses of H-2K(b)-peptide complexes suggest that a conformational adaptation of H-2K(b) drives the decisive step in peptide selection. We propose that MHC class I molecules consider initially a large peptide pool, subsequently refined by a temperature-sensitive induced-fit mechanism to retain the canonical peptide repertoire.

PubMed: 25605945
DOI: 10.1073/pnas.1416543112

Experimental method

X-RAY DIFFRACTION (2.4 Å)