1nfd
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AN ALPHA-BETA T CELL RECEPTOR (TCR) HETERODIMER IN COMPLEX WITH AN ANTI-TCR FAB FRAGMENT DERIVED FROM A MITOGENIC ANTIBODY
OverviewOverview
Each T cell receptor (TCR) recognizes a peptide antigen bound to a major, histocompatibility complex (MHC) molecule via a clonotypic alphabeta, heterodimeric structure (Ti) non-covalently associated with the, monomorphic CD3 signaling components. A crystal structure of an alphabeta, TCR-anti-TCR Fab complex shows an Fab fragment derived from the H57, monoclonal antibody (mAb), interacting with the elongated FG loop of the, Cbeta domain, situated beneath the Vbeta domain. This loop, along with the, partially exposed ABED beta sheet of Cbeta, and glycans attached to both, Cbeta and Calpha domains, forms a cavity of sufficient size to accommodate, a single non-glycosylated Ig domain such as the CD3epsilon ectodomain., That this asymmetrically localized site is embedded within the rigid, constant domain module has implications for the mechanism of signal, transduction in both TCR and pre-TCR complexes. Furthermore, quaternary, structures of TCRs vary significantly even when they bind the same MHC, molecule, as manifested by a unique twisting of the V module relative to, the C module.
About this StructureAbout this Structure
1NFD is a Single protein structure of sequence from Mus musculus with NAG and NDG as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Atomic structure of an alphabeta T cell receptor (TCR) heterodimer in complex with an anti-TCR fab fragment derived from a mitogenic antibody., Wang J, Lim K, Smolyar A, Teng M, Liu J, Tse AG, Liu J, Hussey RE, Chishti Y, Thomson CT, Sweet RM, Nathenson SG, Chang HC, Sacchettini JC, Reinherz EL, EMBO J. 1998 Jan 2;17(1):10-26. PMID:9427737
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