1dqt: Difference between revisions
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'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)''' | '''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)''' | ||
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[[Category: Schwartz, J C.]] | [[Category: Schwartz, J C.]] | ||
[[Category: Shi, W.]] | [[Category: Shi, W.]] | ||
[[Category: | [[Category: Homodimer]] | ||
[[Category: | [[Category: Immunoglobulin variable domain-like beta-sandwich]] | ||
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Revision as of 14:10, 2 May 2008
THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)
OverviewOverview
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.
About this StructureAbout this Structure
1DQT is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of murine CTLA-4 and its role in modulating T cell responsiveness., Ostrov DA, Shi W, Schwartz JC, Almo SC, Nathenson SG, Science. 2000 Oct 27;290(5492):816-9. PMID:11052947 Page seeded by OCA on Fri May 2 14:10:06 2008