1dqt

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(New page: 200px<br /><applet load="1dqt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dqt, resolution 2.0&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1dqt.gif|left|200px]]<br /><applet load="1dqt" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dqt.gif|left|200px]]<br /><applet load="1dqt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dqt, resolution 2.0&Aring;" />
caption="1dqt, resolution 2.0&Aring;" />
'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)'''<br />
'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)'''<br />
==Overview==
==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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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 Structure==
==About this Structure==
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1DQT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CL and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DQT OCA].
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1DQT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQT OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Almo, S.C.]]
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[[Category: Almo, S C.]]
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[[Category: Nathenson, S.G.]]
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[[Category: Nathenson, S G.]]
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[[Category: Ostrov, D.A.]]
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[[Category: Ostrov, D A.]]
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[[Category: Schwartz, J.C.]]
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[[Category: Schwartz, J C.]]
[[Category: Shi, W.]]
[[Category: Shi, W.]]
[[Category: CL]]
[[Category: CL]]
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[[Category: immunoglobulin variable domain-like beta-sandwich]]
[[Category: immunoglobulin variable domain-like beta-sandwich]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:30:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:28 2008''

Revision as of 10:19, 21 February 2008


1dqt, resolution 2.0Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)

Overview

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 Structure

1DQT is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

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:11052947

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