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==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lim, K.]]
[[Category: Lim, K.]]
[[Category: Reinherz, E.L.]]
[[Category: Reinherz, E L.]]
[[Category: Sacchittini, J.]]
[[Category: Sacchittini, J.]]
[[Category: Smolyar, A.]]
[[Category: Smolyar, A.]]
[[Category: Teng, M.K.]]
[[Category: Teng, M K.]]
[[Category: Wang, J.H.]]
[[Category: Wang, J H.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: NDG]]
[[Category: NDG]]
[[Category: complex (immunoreceptor/immunoglobulin)]]
[[Category: complex (immunoreceptor/immunoglobulin)]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:35 2008''

Revision as of 15:05, 21 February 2008

File:1nfd.jpg


1nfd, resolution 2.8Å

Drag the structure with the mouse to rotate

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 and 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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