1bxt
From Proteopedia
(New page: 200px<br /><applet load="1bxt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxt, resolution 1.85Å" /> '''STREPTOCOCCAL SUPERA...) |
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| - | [[Image:1bxt.gif|left|200px]]<br /><applet load="1bxt" size=" | + | [[Image:1bxt.gif|left|200px]]<br /><applet load="1bxt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bxt, resolution 1.85Å" /> | caption="1bxt, resolution 1.85Å" /> | ||
'''STREPTOCOCCAL SUPERANTIGEN (SSA) FROM STREPTOCOCCUS PYOGENES'''<br /> | '''STREPTOCOCCAL SUPERANTIGEN (SSA) FROM STREPTOCOCCUS PYOGENES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Streptococcal superantigen (SSA) is a 28,000 Mr toxin originally isolated | + | Streptococcal superantigen (SSA) is a 28,000 Mr toxin originally isolated from a pathogenic strain of Streptococcus pyogenes that has 60% sequence identity with staphylococcal enterotoxin B (SEB). SSA and SEB, however, do not compete for binding on the surfaces of cells expressing MHC class II molecules. This behavior had been ascribed to SSA and SEB binding to distinct sites on, or different subsets of, HLA-DR molecules. Here we demonstrate that SSA binds predominantly to HLA-DQ, rather than to HLA-DR molecules, and present the crystal structure of SSA at 1.85 A resolution. These data provide a structural basis for interpreting the interaction of SSA with HLA-DQ molecules as well as a foundation for understanding bacterial superantigen affinities for distinct MHC isotypes. |
==About this Structure== | ==About this Structure== | ||
| - | 1BXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http:// | + | 1BXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: toxic shock-like syndrome]] | [[Category: toxic shock-like syndrome]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:14 2008'' |
Revision as of 10:00, 21 February 2008
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STREPTOCOCCAL SUPERANTIGEN (SSA) FROM STREPTOCOCCUS PYOGENES
Overview
Streptococcal superantigen (SSA) is a 28,000 Mr toxin originally isolated from a pathogenic strain of Streptococcus pyogenes that has 60% sequence identity with staphylococcal enterotoxin B (SEB). SSA and SEB, however, do not compete for binding on the surfaces of cells expressing MHC class II molecules. This behavior had been ascribed to SSA and SEB binding to distinct sites on, or different subsets of, HLA-DR molecules. Here we demonstrate that SSA binds predominantly to HLA-DQ, rather than to HLA-DR molecules, and present the crystal structure of SSA at 1.85 A resolution. These data provide a structural basis for interpreting the interaction of SSA with HLA-DQ molecules as well as a foundation for understanding bacterial superantigen affinities for distinct MHC isotypes.
About this Structure
1BXT is a Single protein structure of sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA.
Reference
Structural basis for HLA-DQ binding by the streptococcal superantigen SSA., Sundberg E, Jardetzky TS, Nat Struct Biol. 1999 Feb;6(2):123-9. PMID:10048922
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