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PDBsum entry 1ts3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity.
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Authors
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C.A.Earhart,
D.T.Mitchell,
D.L.Murray,
D.M.Pinheiro,
M.Matsumura,
P.M.Schlievert,
D.H.Ohlendorf.
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Ref.
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Biochemistry, 1998,
37,
7194-7202.
[DOI no: ]
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PubMed id
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Abstract
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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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