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* Residue conservation analysis
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Enzyme class:
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Chains A, B:
E.C.?
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Biochemistry
45:3653-3663
(2006)
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PubMed id:
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Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair.
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A.Yang,
S.Miron,
L.Mouawad,
P.Duchambon,
Y.Blouquit,
C.T.Craescu.
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ABSTRACT
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Human centrin 2 is a component of the nucleotide excision repair system, as a
subunit of the heterotrimer including xeroderma pigmentosum group C protein
(XPC) and hHR23B. The C-terminal domain of centrin (C-HsCen2) binds strongly a
peptide from the XPC protein (P1-XPC: N(847)-R(863)). Here, we characterize the
solution Ca(2+)-dependent structural and molecular features of the C-HsCen2 in
complex with P1-XPC, mainly using NMR spectroscopy and molecular modeling. The
N-terminal half of the peptide, organized as an alpha helix is anchored into a
deep hydrophobic cavity of the protein, because of three bulky hydrophobic
residues in position 1-4-8 and electrostatic contacts with the centrin helix E.
Investigation of the whole centrin interactions shows that the N-terminal domain
of the protein is not involved in the complex formation and is structurally
independent from the peptide-bound C-terminal domain. The complex may exist in
three different binding conformations corresponding to zero, one, and two
Ca(2+)-bound states, which may exchange with various rates and have distinct
structural stability. The various features of the intermolecular interaction
presented here constitute a centrin-specific mode for the target binding.
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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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R.Boutros,
C.Lorenzo,
O.Mondesert,
A.Jauneau,
V.Oakes,
C.Dozier,
B.Gabrielli,
and
B.Ducommun
(2011).
CDC25B associates with a centrin 2-containing complex and is involved in maintaining centrosome integrity.
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Biol Cell,
103,
55-68.
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E.Brun,
Y.Blouquit,
P.Duchambon,
C.Malosse,
J.Chamot-Rooke,
and
C.Sicard-Roselli
(2010).
Oxidative stress induces mainly human centrin 2 polymerisation.
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Int J Radiat Biol,
86,
657-668.
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L.Vugmeyster,
D.Ostrovsky,
and
Y.Li
(2010).
Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant.
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J Biomol NMR,
47,
155-162.
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L.Vugmeyster,
and
C.J.McKnight
(2009).
Phosphorylation-induced changes in backbone dynamics of the dematin headpiece C-terminal domain.
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J Biomol NMR,
43,
39-50.
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D.L.Croteau,
Y.Peng,
and
B.Van Houten
(2008).
DNA repair gets physical: mapping an XPA-binding site on ERCC1.
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DNA Repair (Amst),
7,
819-826.
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L.Chen,
and
K.Madura
(2008).
Centrin/Cdc31 is a novel regulator of protein degradation.
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Mol Cell Biol,
28,
1829-1840.
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P.Trojan,
N.Krauss,
H.W.Choe,
A.Giessl,
A.Pulvermüller,
and
U.Wolfrum
(2008).
Centrins in retinal photoreceptor cells: regulators in the connecting cilium.
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Prog Retin Eye Res,
27,
237-259.
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J.H.Min,
and
N.P.Pavletich
(2007).
Recognition of DNA damage by the Rad4 nucleotide excision repair protein.
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Nature,
449,
570-575.
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PDB codes:
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Y.Blouquit,
P.Duchambon,
E.Brun,
S.Marco,
F.Rusconi,
and
C.Sicard-Roselli
(2007).
High sensitivity of human centrin 2 toward radiolytical oxidation: C-terminal tyrosinyl residue as the main target.
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Free Radic Biol Med,
43,
216-228.
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C.G.Bunick,
M.R.Miller,
B.E.Fuller,
E.Fanning,
and
W.J.Chazin
(2006).
Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein.
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Biochemistry,
45,
14965-14979.
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J.B.Charbonnier,
P.Christova,
A.Shosheva,
E.Stura,
M.H.Le Du,
Y.Blouquit,
P.Duchambon,
S.Miron,
and
C.T.Craescu
(2006).
Crystallization and preliminary X-ray diffraction data of the complex between human centrin 2 and a peptide from the protein XPC.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
649-651.
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J.Martinez-Sanz,
A.Yang,
Y.Blouquit,
P.Duchambon,
L.Assairi,
and
C.T.Craescu
(2006).
Binding of human centrin 2 to the centrosomal protein hSfi1.
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FEBS J,
273,
4504-4515.
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
