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PDBsum entry 2kqc
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References listed in PDB file
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Key reference
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Title
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Solution structures of the two pbz domains from human aplf and their interaction with poly(ADP-Ribose).
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Authors
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S.Eustermann,
C.Brockmann,
P.V.Mehrotra,
J.C.Yang,
D.Loakes,
S.C.West,
I.Ahel,
D.Neuhaus.
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Ref.
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Nat Struct Biol, 2010,
17,
241-243.
[DOI no: ]
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PubMed id
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Abstract
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Addition of poly(ADP-ribose) (PAR) is an important post-translational
modification in higher eukaryotes. Several DNA repair and checkpoint proteins
possess specific PAR-binding zinc-finger (PBZ) modules critical for function.
Here, we present solution structures of the two PBZ modules of aprataxin and
PNK-like factor (APLF), revealing a novel type of zinc finger. By combining in
vivo PAR-binding data with NMR interaction data using PAR fragments, we propose
a structural basis for PBZ-PAR recognition.
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Figure 1.
(a) Domain architecture and partial sequence of human APLF.
The PBZ modules (F1 and F2) are boxed, metal-binding residues
are pink, key PAR-binding residues are violet and the additional
loop of F1 is orange. Highly conserved residues are bold
(Supplementary Fig. 11), and asterisks indicate residues mutated
in our study. (b) Solution structures of APLF F1 and F2, colored
as in a with zinc ions as blue spheres and helices dark red; the
ten lowest-energy structures are shown. Structural statistics
appear in Supplementary Table 1 and Supplementary Figure 2.
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Figure 2.
(a) Structure of PAR and fragments; ADPR is the fragment
within the gray area and RFA is that within the blue area (the
darker blue area being common to both). The labels "protein" and
"distal" are purely to indicate chain direction. (b,c)
Structures of RFA bound to APLF F1 (b) and APLF F2 (c). In b,
the RFA molecule is schematically extended to show how PAR may
bind; c shows a close-up of key interactions (including H-bond
adenosyl NH[2]–S426 O, dotted line).
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2010,
17,
241-243)
copyright 2010.
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