2qil

<StructureSection load='2qil' size='340' side='right' caption='[[2qil]], [[Resolution|resolution]] 2.07&Aring;' scene=''>

<table><tr><td colspan='2'>[[2qil]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIL OCA]. <br>

</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qil OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qil RCSB], [http://www.ebi.ac.uk/pdbsum/2qil PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qi/2qil_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The pyrogenic toxin toxic shock syndrome toxin-1 from Staphylococcus aureus is a causative agent of the toxic shock syndrome disease. It belongs to a family of proteins known as superantigens that cross-link major histocompatibility class II molecules and T-cell receptors leading to the activation of a substantial number of T cells. The crystal structure of this protein has been refined to 2.07 A with an Rcryst value of 20.4% for 51,240 reflections. The final model contains three molecules in the asymmetric unit with good stereochemistry and a root-mean-square deviation of 0.009 A and 1.63 from ideality for bond lengths and bond angles, respectively. The overall fold is considerably similar to that of other known microbial superantigens (staphylococcal enterotoxins). However, a detailed structural analysis shows that toxic shock syndrome toxin-1 lacks several structural features that affect its specificity for V beta elements of the T-cell receptor and also its recognition by major histocompatibility class II molecules.

The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 A resolution.,Papageorgiou AC, Brehm RD, Leonidas DD, Tranter HS, Acharya KR J Mol Biol. 1996 Jul 26;260(4):553-69. PMID:8759320<ref>PMID:8759320</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Acharya, K R.]]

[[Category: Papageorgiou, A C.]]

[[Category: Toxic shock syndrome toxin]]