1DQT: THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)

Citation:
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.
PDB ID: 1DQTDownload
MMDB ID: 14758
PDB Deposition Date: 2000/1/5
Updated in MMDB: 2000/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1DQT: dimeric; determined by author and by software (PISA)
Molecular Components in 1DQT
Label Count Molecule
Proteins (2 molecules)
2
Cytotoxic T Lymphocyte Associated Antigen 4(Gene symbol: Ctla4)
Molecule annotation
Chemicals (5 molecules)
1
4
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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