1dqt: Difference between revisions
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[[Image:1dqt.gif|left|200px]] | [[Image:1dqt.gif|left|200px]] | ||
'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)''' | {{Structure | ||
|PDB= 1dqt |SIZE=350|CAPTION= <scene name='initialview01'>1dqt</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DQT is a [ | 1DQT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQT OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11052947 11052947] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immunoglobulin variable domain-like beta-sandwich]] | [[Category: immunoglobulin variable domain-like beta-sandwich]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:52 2008'' |
Revision as of 11:42, 20 March 2008
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, resolution 2.0Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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
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