1DQT

THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)

Summary for 1DQT

• Entry DOI: 10.2210/pdb1dqt/pdb
• Descriptor: CYTOTOXIC T LYMPHOCYTE ASSOCIATED ANTIGEN 4, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: immunoglobulin variable domain-like beta-sandwich, homodimer, immune system
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane ; Single-pass type I membrane protein : P09793
• Total number of polymer chains: 4
• Total formula weight: 51914.06

Authors

Ostrov, D.A.,Shi, W.,Schwartz, J.C.,Almo, S.C.,Nathenson, S.G. (deposition date: 2000-01-05, release date: 2000-10-27, Last modification date: 2024-10-30)

Primary citation

Ostrov, D.A.,Shi, W.,Schwartz, J.C.,Almo, S.C.,Nathenson, S.G.
Structure of murine CTLA-4 and its role in modulating T cell responsiveness.
Science, 290:816-819, 2000

PubMed Abstract: 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.

PubMed: 11052947
DOI: 10.1126/science.290.5492.816

Experimental method

X-RAY DIFFRACTION (2 Å)