T-cell receptor

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[[Image:2xna.png|left|200px|thumb|hTCR α+β chains + enterotoxin, [[2xna]]]]
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{{STRUCTURE_2xna| PDB=2xna | SIZE=400| SCENE= |right|CAPTION= T-cell receptor α chain (grey), β chain (green) complex with enterotoxin (pink), glycerol and Na+ ion (purple) [[2xna]].}}
{{STRUCTURE_2xna| PDB=2xna | SIZE=400| SCENE= |right|CAPTION= T-cell receptor α chain (grey), β chain (green) complex with enterotoxin (pink), glycerol and Na+ ion (purple) [[2xna]].}}
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'''T-cell receptors''' (TCR) reside on the surface of T lymphocytes. TCR recognizes antigens bound to major histocompatibility complex (MHC) molecules. The binding of TCR to the antigen-MHC activates the T lymphocytes. TCR is a heterodimer α+β and ca. 5% the T cells have a γ+δ heterodimer. For more details see [[SP3.4-TCR-HLA-DQ8-∝-1-gliadin_complex]].
'''T-cell receptors''' (TCR) reside on the surface of T lymphocytes. TCR recognizes antigens bound to major histocompatibility complex (MHC) molecules. The binding of TCR to the antigen-MHC activates the T lymphocytes. TCR is a heterodimer α+β and ca. 5% the T cells have a γ+δ heterodimer. For more details see [[SP3.4-TCR-HLA-DQ8-∝-1-gliadin_complex]].

Revision as of 10:58, 20 August 2014

Template:STRUCTURE 2xna

T-cell receptors (TCR) reside on the surface of T lymphocytes. TCR recognizes antigens bound to major histocompatibility complex (MHC) molecules. The binding of TCR to the antigen-MHC activates the T lymphocytes. TCR is a heterodimer α+β and ca. 5% the T cells have a γ+δ heterodimer. For more details see SP3.4-TCR-HLA-DQ8-∝-1-gliadin_complex.

Contents

3D structures of T-cell receptor

Updated on 20-August-2014

TCR α chain

1ac6, 1b88, 1h5b, 1i9e – mTCR α chain variable domain - mouse

TCR β chain

1bec – mTCR β chain
2axh – hTCR β chain (mutant) - human
2axj – hTCR β chain
2apb, 2apf, 2apt, 2apv, 2apw, 2apx – TCR β chain (mutant) - rat

TCR β chain + antigen

1jck, 1sbb, 1l0x, 1l0y, 2aq1, 2aq2, 2aq3, 3mc0 – mTCR β chain (mutant) + antigen
1ktk, 3byt, 3byy, 3bzd – hTCR β chain (mutant) + exotoxin type C
2ij0 – hTCR β chain + toxic shock syndrome toxin-1

TCR δ chain

1tvd – hTCR δ chain variable domain

TCR α+β chains

1tcr, 2z35 – mTCR α+β chains
1tcr, 2q86 – mTCR α+β chains (mutant)
1bwm – mTCR α+β chains variable domains (mutant) - NMR
1kgc, 2nw2, 2vlm, 3dx9, 3mff, 3qeu, 3skn, 4dzb, 4e42, 4jfh, 4g8f, 4g8e – hTCR α+β chains
4ei6 – h/mTCR α+β chains
2ial, 4gg8 – hTCR α+β chains (mutant)
3of6 – hTCR pre-α+β (mutant) chains

TCR γ+δ chains

1hxm, 3omz – hTCR γ+δ chains

TCR complex with antigen

1nfd, 1kb5 – mTCR α+β chains + FAB fragment
2xna – hTCR α+β chains + enterotoxin

TCR complex with MHC and antigen

1ao7, 1bd2, 1qrn, 1qse, 1qsf, 1mi5, 1oga, 1lp9, 2bnq, 2bnr, 2bnu, 2ak4, 2esv, 2f53, 2f54, 2gj6, 2nx5, 2p5e, 2p5w, 2pye, 2pyf, 3dxa, 3hg1, 3gsn, 3kpr, 3kps, 3kxf, 3o4l, 3qdg, 3qdj, 3qdm, 3qeq, 3sjv, 2ypl, 4jff, 4jfe, 4jfd, 4jry, 4jrx – hTCR α+β chains + MHC + β-2 microglobulin + polypeptide
1fyt, 1ymm, 1zgl, 4e41 – hTCR α+β chains + MHC + polypeptide
3o6f – hTCR α+β chains + MHC
3pl6 – hTCR α chain + MHC + polypeptide
2xn9 – hTCR α+β chains + MHC + polypeptide + enterotoxin
3huj, 3vwj, 3vwk – hTCR α+β chains + β-2 microglobulin + CD1D
3tzv – hTCR α+β chains (mutant) + β-2 microglobulin + CD1D
3t0e – hTCR α+β chains + MHC + CD4
3o8x, 3o9w, 4ei5 – h/mTCR α+β chains + β-2 microglobulin + CD1D
3scm, 3sda, 3sdc, 3sdd, 3sdx – h/mTCR α+β chains + β-2 microglobulin + CD1D + ceramide derivative
2iam, 2ian – hTCR α+β chains (mutant) + MHC + polypeptide
1j8h, 4gg6 – hTCR α+β chains (mutant) + MHC + polypeptide
2ckb, 1fo0, 1g6r, 1kj2, 1mwa, 1nam, 2ol3, 2j8u – mTCR α+β chains + MHC + β-2 microglobulin + polypeptide
2pxy – mTCR α+β chains (mutant) + MHC + β-2 microglobulin + polypeptide
2icw – mTCR α+β chains + MHC + mycoplasma arthritidis mitogen + polypeptide
1d9k, 2e7l, 2oi9, 2z31, 3e2h, 3e3q, 3qib – mTCR α+β chains + MHC + polypeptide
1u3h – mTCR α+β chains (mutant) + MHC + polypeptide
1ypz – hTCR γ+δ chains + MHC + β-2 microglobulin

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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