Ontology highlight
ABSTRACT:
SUBMITTER: Ghendler Y
PROVIDER: S-EPMC2212265 | biostudies-literature | 1998 May
REPOSITORIES: biostudies-literature
Ghendler Y Y Smolyar A A Chang H C HC Reinherz E L EL
The Journal of experimental medicine 19980501 9
A recent crystal structure of the N15 alpha/beta-T cell receptor (TCR) in complex with an Fab derived from the H57 Cbeta-specific monoclonal antibody (mAb) shows the mAb fragment interacting with the elongated FG loop of the Cbeta domain. This loop creates one side wall of a cavity within the TCR Ti-alpha/beta constant region module (CalphaCbeta) while the CD and EF loops of the Calpha domain form another wall. The cavity size is sufficient to accommodate a single nonglycosylated Ig domain such ...[more]