2gto
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Oxidized form of ADAP hSH3-N
OverviewOverview
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.
About this StructureAbout this Structure
2GTO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Redox-Regulated Conformational Changes in an SH3 Domain(,)., Zimmermann J, Kuhne R, Sylvester M, Freund C, Biochemistry. 2007 Jun 12;46(23):6971-7. Epub 2007 May 19. PMID:17511475
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