Article
The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity.
Immunity - 1 Mar 2001
Rudolph M G, Speir J A, Brunmark A, Mattsson N, Jackson M R, Peterson P A, Teyton L, Wilson I A
Abstract excerpt
The K(bm1) and K(bm8) natural mutants of the murine MHC class I molecule H-2K(b) were originally identified by allograft rejection. They also bind viral peptides VSV8 and SEV9 with high affinity, but their peptide complexes have substantially decreased thermostability, and the K(bm1) complexes do not elicit alloreactive T cell responses. Crystal structures of the four mutant complexes at 1.7-1.9 A resolution are...
Topics
- Animals
- Antigen Presentation
- Binding Sites
- Crystallography, X-Ray
- Epitopes
- H-2 Antigens
- Half-Life
- Mice
- Models, Molecular
- Mutation
- Peptides
- Protein Conformation
- Static Electricity
- Surface Properties