 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](nw5071fig1mag.jpg)
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Figure 1
(a) Amino-acid sequences of APIM and PIPM. An asterisk indicates the C-terminus. Numbers above the PIPM sequences indicate the positions of the amino acids in the motif. Positions crucial for interaction with PCNA are shown in red. Note that the residue numbering of Pol-ι refers to the UniProtKB sequence (Q9UNA4) and differs from that used in a previous structural study, where the N-terminal 25 residues were missing (Hishiki et al., 2009  ). (b) Domain architecture of human ZRANB3. Human ZRANB3 consists of an SNF2 helicase domain, PIPM, an NZF ubiquitin-binding domain, an HPL (HARP-like) domain, an HNH nuclease motif and APIM. Both PCNA-interacting motifs, PIPM and APIM, make significant contribution to PCNA-dependent recruitment of ZRANB3 to DNA-damage sites, whereas the functional difference between the PIPM and APIM of ZRANB3 in the recruitment is unclarified. The peptide sequence of the human ZRANB3 APIM used in this crystallographic study is shown at the bottom of the domain architecture and the consensus APIM residues are shown in red. |
![[Figure 1]](nw5071fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
