1dr9
From Proteopedia
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- | [[Image:1dr9.gif|left|200px]] | + | [[Image:1dr9.gif|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)''' | + | {{Structure |
+ | |PDB= 1dr9 |SIZE=350|CAPTION= <scene name='initialview01'>1dr9</scene>, resolution 3.00Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= CHO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1DR9 is a [ | + | 1DR9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DR9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10661405 10661405] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ig superfamily]] | [[Category: ig superfamily]] | ||
- | ''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 10:43:03 2008'' |
Revision as of 08:43, 20 March 2008
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, resolution 3.00Å | |||||||
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Ligands: | |||||||
Gene: | CHO (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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