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1yjd
From Proteopedia
(New page: 200px<br /> <applet load="1yjd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yjd, resolution 2.700Å" /> '''Crystal structure ...) |
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| - | [[Image:1yjd.gif|left|200px]]<br /> | + | [[Image:1yjd.gif|left|200px]]<br /><applet load="1yjd" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yjd" size=" | + | |
caption="1yjd, resolution 2.700Å" /> | caption="1yjd, resolution 2.700Å" /> | ||
'''Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)'''<br /> | '''Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Naive T cell activation requires signaling by the T cell receptor and by | + | Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system. |
==About this Structure== | ==About this Structure== | ||
| - | 1YJD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YJD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJD OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Davis, S | + | [[Category: Davis, S J.]] |
| - | [[Category: Esnouf, R | + | [[Category: Esnouf, R M.]] |
| - | [[Category: Evans, E | + | [[Category: Evans, E J.]] |
| - | [[Category: Gilbert, R | + | [[Category: Gilbert, R J.C.]] |
| - | [[Category: James, J | + | [[Category: James, J R.]] |
[[Category: Manso-Sancho, R.]] | [[Category: Manso-Sancho, R.]] | ||
[[Category: Sorensen, P.]] | [[Category: Sorensen, P.]] | ||
| - | [[Category: Stuart, D | + | [[Category: Stuart, D I.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: cd28 homodimer]] | [[Category: cd28 homodimer]] | ||
[[Category: igsf]] | [[Category: igsf]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:55 2008'' |
Revision as of 14:05, 21 February 2008
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Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)
Overview
Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system.
About this Structure
1YJD is a Single protein structure of sequence from Homo sapiens and Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a soluble CD28-Fab complex., Evans EJ, Esnouf RM, Manso-Sancho R, Gilbert RJ, James JR, Yu C, Fennelly JA, Vowles C, Hanke T, Walse B, Hunig T, Sorensen P, Stuart DI, Davis SJ, Nat Immunol. 2005 Mar;6(3):271-9. Epub 2005 Feb 6. PMID:15696168
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