title: Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein.
abstract: RecQ C-terminal (RQC) domain is known as the main DNA binding module of RecQ helicases such as Bloom syndrome protein (BLM) and Werner syndrome protein (WRN) that recognizes various DNA structures. Even though BLM is able to resolve various DNA structures similarly to WRN, BLM has different binding preferences for DNA substrates from WRN. In this study, we determined the solution structure of the RQC domain of human BLM. The structure shares the common winged-helix motif with other RQC domains. However, half of the N-terminal has unstructured regions (α1-α2 loop and α3 region), and the aromatic side chain on the top of the β-hairpin, which is important for DNA duplex strand separation in other RQC domains, is substituted with a negatively charged residue (D1165) followed by the polar residue (Q1166). The structurally distinctive features of the RQC domain of human BLM suggest that the DNA binding modes of the BLM RQC domain may be different from those of other RQC domains.
authors.affiliation: Division of Liberal Arts and Sciences, Department of Chemistry, Gwangju Institute of Science and Technology, Oryong-dong, Buk-gu, Gwangju, 500-712, Republic of Korea, cjpark@gist.ac.kr.
authors.forename: Chin-Ju
authors.initials: CJ
authors.lastname: Park
authors.forename: Junsang
authors.initials: J
authors.lastname: Ko
authors.forename: Kyoung-Seok
authors.initials: KS
authors.lastname: Ryu
authors.forename: Byong-Seok
authors.initials: BS
authors.lastname: Choi
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D053484:RecQ Helicases / Q000737:chemistry*; D016415:Sequence Alignment; D012996:Solutions
chemical_list: D012996:Solutions; C097151:Bloom syndrome protein; D053484:RecQ Helicases