2ici

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[[Image:2ici.gif|left|200px]]<br /><applet load="2ici" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ici.gif|left|200px]]
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caption="2ici, resolution 1.560&Aring;" />
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'''Crystal Structure of Streptococcal Pyrogenic Exotoxin I'''<br />
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{{Structure
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|PDB= 2ici |SIZE=350|CAPTION= <scene name='initialview01'>2ici</scene>, resolution 1.560&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|ACTIVITY=
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|GENE= speI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1314 Streptococcus pyogenes])
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}}
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'''Crystal Structure of Streptococcal Pyrogenic Exotoxin I'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ICI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ICI OCA].
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2ICI is a [[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=2ICI OCA].
==Reference==
==Reference==
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Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens., Brouillard JN, Gunther S, Varma AK, Gryski I, Herfst CA, Rahman AK, Leung DY, Schlievert PM, Madrenas J, Sundberg EJ, McCormick JK, J Mol Biol. 2007 Apr 6;367(4):925-34. Epub 2007 Jan 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17303163 17303163]
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Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens., Brouillard JN, Gunther S, Varma AK, Gryski I, Herfst CA, Rahman AK, Leung DY, Schlievert PM, Madrenas J, Sundberg EJ, McCormick JK, J Mol Biol. 2007 Apr 6;367(4):925-34. Epub 2007 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17303163 17303163]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
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[[Category: streptococcal superantigen spei]]
[[Category: streptococcal superantigen spei]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:53 2008''

Revision as of 15:27, 20 March 2008


PDB ID 2ici

Drag the structure with the mouse to rotate
, resolution 1.560Å
Ligands:
Gene: speI (Streptococcus pyogenes)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Streptococcal Pyrogenic Exotoxin I


Overview

Superantigens (SAgs) are potent microbial toxins that bind simultaneously to T cell receptors (TCRs) and class II major histocompatibility complex molecules, resulting in the activation and expansion of large T cell subsets and the onset of numerous human diseases. Within the bacterial SAg family, streptococcal pyrogenic exotoxin I (SpeI) has been classified as belonging to the group V SAg subclass, which are characterized by a unique, relatively conserved approximately 15 amino acid extension (amino acid residues 154 to 170 in SpeI; herein referred to as the alpha3-beta8 loop), absent in SAg groups I through IV. Here, we report the crystal structure of SpeI at 1.56 A resolution. Although the alpha3-beta8 loop in SpeI is several residues shorter than that of another group V SAg, staphylococcal enterotoxin serotype I, the C-terminal portions of these loops, which are located adjacent to the putative TCR binding site, are structurally similar. Mutagenesis and subsequent functional analysis of SpeI indicates that TCR beta-chains are likely engaged in a similar general orientation as other characterized SAgs. We show, however, that the alpha3-beta8 loop length, and the presence of key glycine residues, are necessary for optimal activation of T cells. Based on Vbeta-skewing analysis of human T cells activated with SpeI and structural models, we propose that the alpha3-beta8 loop is positioned to form productive intermolecular contacts with the TCR beta-chain, likely in framework region 3, and that these contacts are required for optimal TCR recognition by SpeI, and likely all other group V SAgs.

About this Structure

2ICI is a Single protein structure of sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA.

Reference

Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens., Brouillard JN, Gunther S, Varma AK, Gryski I, Herfst CA, Rahman AK, Leung DY, Schlievert PM, Madrenas J, Sundberg EJ, McCormick JK, J Mol Biol. 2007 Apr 6;367(4):925-34. Epub 2007 Jan 12. PMID:17303163

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