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PDBsum entry 2gto
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Signaling protein
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PDB id
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2gto
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References listed in PDB file
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Key reference
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Title
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Redox-Regulated conformational changes in an sh3 domain.
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Authors
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J.Zimmermann,
R.Kühne,
M.Sylvester,
C.Freund.
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Ref.
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Biochemistry, 2007,
46,
6971-6977.
[DOI no: ]
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PubMed id
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Abstract
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Oxidation-induced conformational changes in proteins provide a powerful
mechanism to sense the redox state of a living cell. In contrast to the
unspecific and often irreversible oxidation of intracellular proteins during
severe oxidative stress, regulatory redox events need to have specific and
transient effects on cellular targets. Here we present evidence for the
reversible formation of a vicinal disulfide bond in a prototypic protein
interaction domain. NMR spectroscopy was used to determine the structure of the
N-terminal hSH3 domain (hSH3N) of the immune cell protein ADAP (adhesion and
degranulation promoting adapter protein) in the reduced and oxidized states. An
eight-membered ring formed upon oxidation of two neighboring cysteines leads to
significant changes in the variable arginine-threonine (RT) loop of the hSH3N
domain and alters the helix-sheet packing of the domain. The redox potential for
this structural transition is -228 mV at pH 7.4. This is compatible with a role
of the cysteinylcysteine moiety in redox signaling during T cell activation.
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Secondary reference #1
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Title
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Nmr assignment of the reduced and oxidized forms of the human adap hsh3-1 domain.
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Authors
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J.Zimmermann,
C.Freund.
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Ref.
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J Biomol Nmr, 2005,
32,
94.
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PubMed id
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