Research Paper Volume 4, Issue 6 pp 417—429
DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities
Figure 1. Structure and mutation sites of WRN helicase.
(A) Domain structure of WRN. Functional domains are indicated below the structure. (B) Amino acid sequence alignment of RQC domain of RecQ helicases. Human WRN RQC (WRN), human BLM RQC (BLM), human RECQL1 RQC (RECQ1) and E. coli RecQ RQC (eRECQ) are shown. Secondary structures of WRN RQC domain are represented below the sequences. ▼ indicates DNA-contacting amino acid residues in WRN RQC-DNA complex (PDB ID: 3AAF). Mutated sites indicated with broken line box. (C) Structure of WRN RQC-DNA complex (PDB ID: 3AAF). The figure generated using PyMOL (DeLano,