1dr9

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(New page: 200px<br /> <applet load="1dr9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dr9, resolution 3.00&Aring;" /> '''CRYSTAL STRUCTURE O...)
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<applet load="1dr9" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1dr9, resolution 3.00&Aring;" />
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'''CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)'''<br />
'''CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)'''<br />
==Overview==
==Overview==
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B7-1 (CD80) and B7-2 (CD86) are glycoproteins expressed on, antigen-presenting cells. The binding of these molecules to the T cell, homodimers CD28 and CTLA-4 (CD152) generates costimulatory and inhibitory, signals in T cells, respectively. The crystal structure of the, extracellular region of B7-1 (sB7-1), solved to 3 A resolution, consists, of a novel combination of two Ig-like domains, one characteristic of, adhesion molecules and the other previously seen only in antigen, receptors. In the crystal lattice, sB7-1 unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. Analytical ultracentrifugation, reveals that sB7-1 also dimerizes in solution. The structural data suggest, a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4, homodimers, along with the relatively high affinity of these interactions, favors the formation of very stable inhibitory signaling complexes.
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B7-1 (CD80) and B7-2 (CD86) are glycoproteins expressed on antigen-presenting cells. The binding of these molecules to the T cell homodimers CD28 and CTLA-4 (CD152) generates costimulatory and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-1), solved to 3 A resolution, consists of a novel combination of two Ig-like domains, one characteristic of adhesion molecules and the other previously seen only in antigen receptors. In the crystal lattice, sB7-1 unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. Analytical ultracentrifugation reveals that sB7-1 also dimerizes in solution. The structural data suggest a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4 homodimers, along with the relatively high affinity of these interactions, favors the formation of very stable inhibitory signaling complexes.
==About this Structure==
==About this Structure==
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1DR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DR9 OCA].
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1DR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1DR9 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davis, S.J.]]
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[[Category: Davis, S J.]]
[[Category: Ikemizu, S.]]
[[Category: Ikemizu, S.]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: ig superfamily]]
[[Category: ig superfamily]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:35:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:37 2008''

Revision as of 10:19, 21 February 2008


1dr9, resolution 3.00Å

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CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)

Overview

B7-1 (CD80) and B7-2 (CD86) are glycoproteins expressed on antigen-presenting cells. The binding of these molecules to the T cell homodimers CD28 and CTLA-4 (CD152) generates costimulatory and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-1), solved to 3 A resolution, consists of a novel combination of two Ig-like domains, one characteristic of adhesion molecules and the other previously seen only in antigen receptors. In the crystal lattice, sB7-1 unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. Analytical ultracentrifugation reveals that sB7-1 also dimerizes in solution. The structural data suggest a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4 homodimers, along with the relatively high affinity of these interactions, favors the formation of very stable inhibitory signaling complexes.

About this Structure

1DR9 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure and dimerization of a soluble form of B7-1., Ikemizu S, Gilbert RJ, Fennelly JA, Collins AV, Harlos K, Jones EY, Stuart DI, Davis SJ, Immunity. 2000 Jan;12(1):51-60. PMID:10661405

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