1ts2: Difference between revisions
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[[Image: | ==T128A MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS== | ||
<StructureSection load='1ts2' size='340' side='right' caption='[[1ts2]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ts2]] 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=1TS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TS2 FirstGlance]. <br> | |||
</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=1ts2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ts2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ts2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ts2 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ts/1ts2_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three-dimensional structures of five mutants of toxic shock syndrome toxin-1 (TSST-1) have been determined. These mutations are in the long central alpha helix and are useful in mapping portions of TSST-1 involved in superantigenicity and lethality. The T128A, H135A, Q139K, and I140T mutations appear to reduce superantigenicity by altering the properties of the T-cell receptor interaction surface. The Q136A mutation is at a largely buried site and causes a dramatic change in the conformation of the beta7-beta9 loop which covers the back of the central alpha helix. As this mutation has the unique ability to reduce the toxin's lethality in rabbits while retaining its superantigenicity, it raises the possibility that this rear loop mediates the ability of TSST-1 to induce lethality and suggests a route for producing nonlethal toxins for therapeutic development. | |||
Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity.,Earhart CA, Mitchell DT, Murray DL, Pinheiro DM, Matsumura M, Schlievert PM, Ohlendorf DH Biochemistry. 1998 May 19;37(20):7194-202. PMID:9585531<ref>PMID:9585531</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Earhart, C A.]] | [[Category: Earhart, C A.]] | ||
Revision as of 21:37, 29 September 2014
T128A MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUST128A MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structures of five mutants of toxic shock syndrome toxin-1 (TSST-1) have been determined. These mutations are in the long central alpha helix and are useful in mapping portions of TSST-1 involved in superantigenicity and lethality. The T128A, H135A, Q139K, and I140T mutations appear to reduce superantigenicity by altering the properties of the T-cell receptor interaction surface. The Q136A mutation is at a largely buried site and causes a dramatic change in the conformation of the beta7-beta9 loop which covers the back of the central alpha helix. As this mutation has the unique ability to reduce the toxin's lethality in rabbits while retaining its superantigenicity, it raises the possibility that this rear loop mediates the ability of TSST-1 to induce lethality and suggests a route for producing nonlethal toxins for therapeutic development. Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity.,Earhart CA, Mitchell DT, Murray DL, Pinheiro DM, Matsumura M, Schlievert PM, Ohlendorf DH Biochemistry. 1998 May 19;37(20):7194-202. PMID:9585531[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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