 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](no5058fig4mag.jpg)
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Figure 4
Binding of BMN 673 at the extended binding pocket. (a) Structural variability of the D-loop illustrated on superimposed crystallographic structures of PARP3 (PDB entry 3fhb ; Lehtiö et al., 2009  ), tankyrase 1 (2rf5
; Lehtiö et al., 2008) and tankyrase 2 (3kr7
; Karlberg, Markova et al., 2010), PARP1 and PARP2. (b) Unlike the other PARP1 inhibitors shown in cyan [PDB entries 1uk1
(Hattori et al., 2004), 1uk0
(Kinoshita et al., 2004), 3gjw
(Miyashiro et al., 2009), 4hhz
(Ye et al., 2013) and 4l6s
(Gangloff et al., 2013)] and orange [PDB entries 1wok
(Iwashita et al., 2005), 2rd6
, 2rcw
and 3gn7
(C. R. Park, unpublished work), 3l3m
(Penning et al., 2010), 3l3l
(Gandhi et al., 2010) and 4gv7
(Lindgren et al., 2013)] which are directed towards sub-sites 1 and 2, a disubstituted BMN 673 molecule occupies a unique space within the extended NAD+-binding pocket. |
![[Figure 4]](no5058fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
