1dqt: Difference between revisions

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{{STRUCTURE_1dqt|  PDB=1dqt  |  SCENE=  }}  
{{STRUCTURE_1dqt|  PDB=1dqt  |  SCENE=  }}  


'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)'''
===THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)===




==Overview==
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The effective regulation of T cell responses is dependent on opposing signals transmitted through two related cell-surface receptors, CD28 and cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). Dimerization of CTLA-4 is required for the formation of high-avidity complexes with B7 ligands and for transmission of signals that attenuate T cell activation. We determined the crystal structure of the extracellular portion of CTLA-4 to 2.0 angstrom resolution. CTLA-4 belongs to the immunoglobulin superfamily and displays a strand topology similar to Valpha domains, with an unusual mode of dimerization that places the B7 binding sites distal to the dimerization interface. This organization allows each CTLA-4 dimer to bind two bivalent B7 molecules and suggests that a periodic arrangement of these components within the immunological synapse may contribute to the regulation of T cell responsiveness.
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==About this Structure==
==About this Structure==
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[[Category: Homodimer]]
[[Category: Homodimer]]
[[Category: Immunoglobulin variable domain-like beta-sandwich]]
[[Category: Immunoglobulin variable domain-like beta-sandwich]]
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