Ontology highlight
ABSTRACT:
SUBMITTER: Natarajan K
PROVIDER: S-EPMC5440810 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
Nature communications 20170516
The molecular mechanism through which the interaction of a clonotypic αβ T-cell receptor (TCR) with a peptide-loaded major histocompatibility complex (p/MHC) leads to T-cell activation is not yet fully understood. Here we exploit a high-affinity TCR (B4.2.3) to examine the structural changes that accompany binding to its p/MHC ligand (P18-I10/H2-D<sup>d</sup>). In addition to conformational changes in complementarity-determining regions (CDRs) of the TCR seen in comparison of unliganded and boun ...[more]