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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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Contents |
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* Residue conservation analysis
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PDB id:
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Signaling protein
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Title:
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Oxidized form of adap hsh3-n
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Structure:
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Fyn-binding protein. Chain: a. Fragment: hsh3-n (oxidized). Synonym: adap, fyn-t-binding protein, fyb-120/130, p120/p130, slp-76- associated phosphoprotein, slap-130. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: fyb, slap130. Expressed in: escherichia coli. Expression_system_taxid: 562
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NMR struc:
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20 models
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Authors:
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C.Freund,J.Zimmermann,R.Kuehne
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Key ref:
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J.Zimmermann
et al.
(2007).
Redox-regulated conformational changes in an SH3 domain.
Biochemistry,
46,
6971-6977.
PubMed id:
DOI:
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Date:
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28-Apr-06
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Release date:
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05-Jun-07
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PROCHECK
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Headers
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References
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O15117
(FYB1_HUMAN) -
FYN-binding protein 1 from Homo sapiens
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Seq:
Struc:
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783 a.a.
96 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Biochemistry
46:6971-6977
(2007)
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PubMed id:
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Redox-regulated conformational changes in an SH3 domain.
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J.Zimmermann,
R.Kühne,
M.Sylvester,
C.Freund.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Sylvester,
S.Kliche,
S.Lange,
S.Geithner,
C.Klemm,
A.Schlosser,
A.Grossmann,
U.Stelzl,
B.Schraven,
E.Krause,
and
C.Freund
(2010).
Adhesion and degranulation promoting adapter protein (ADAP) is a central hub for phosphotyrosine-mediated interactions in T cells.
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PLoS One,
5,
e11708.
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A.L.Skinner,
A.A.Vartia,
T.D.Williams,
and
J.S.Laurence
(2009).
Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.
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Biochemistry,
48,
4262-4272.
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B.J.Burbach,
R.Srivastava,
R.B.Medeiros,
W.E.O'Gorman,
E.J.Peterson,
and
Y.Shimizu
(2008).
Distinct regulation of integrin-dependent T cell conjugate formation and NF-kappa B activation by the adapter protein ADAP.
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J Immunol,
181,
4840-4851.
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K.Piotukh,
D.Kosslick,
J.Zimmermann,
E.Krause,
and
C.Freund
(2007).
Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy.
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Free Radic Biol Med,
43,
1263-1270.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
