1ts3

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(New page: 200px<br /><applet load="1ts3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ts3, resolution 2.0&Aring;" /> '''H135A MUTANT OF TOXIC...)
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[[Image:1ts3.gif|left|200px]]<br /><applet load="1ts3" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ts3.gif|left|200px]]<br /><applet load="1ts3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ts3, resolution 2.0&Aring;" />
caption="1ts3, resolution 2.0&Aring;" />
'''H135A MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS'''<br />
'''H135A MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1TS3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TS3 OCA].
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1TS3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1TS3 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Earhart, C.A.]]
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[[Category: Earhart, C A.]]
[[Category: Matsumura, M.]]
[[Category: Matsumura, M.]]
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[[Category: Mitchell, D.T.]]
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[[Category: Mitchell, D T.]]
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[[Category: Murray, D.L.]]
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[[Category: Murray, D L.]]
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[[Category: Ohlendorf, D.H.]]
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[[Category: Ohlendorf, D H.]]
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[[Category: Pinheiro, D.M.]]
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[[Category: Pinheiro, D M.]]
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[[Category: Schlievert, P.M.]]
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[[Category: Schlievert, P M.]]
[[Category: superantigen]]
[[Category: superantigen]]
[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:33:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:44 2008''

Revision as of 13:16, 21 February 2008


1ts3, resolution 2.0Å

Drag the structure with the mouse to rotate

H135A MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS

Overview

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.

About this Structure

1TS3 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

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

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