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PDBsum entry 2a4j
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Structural protein
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PDB id
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2a4j
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References listed in PDB file
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Key reference
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Title
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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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Authors
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A.Yang,
S.Miron,
L.Mouawad,
P.Duchambon,
Y.Blouquit,
C.T.Craescu.
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Ref.
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Biochemistry, 2006,
45,
3653-3663.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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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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