Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein

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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 (alpha 1-alpha 2 loop and alpha 3 region), and the aromatic side chain on the top of the beta-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.
Publisher
SPRINGER
Issue Date
2014-02
Language
English
Article Type
Article
Keywords

WERNER-SYNDROME PROTEIN; STRAND-SEPARATION; HRDC DOMAIN; DNA-BINDING; NMR SYSTEM; CRYSTALLOGRAPHY; HELICASES; WRN

Citation

JOURNAL OF BIOMOLECULAR NMR, v.58, no.2, pp.141 - 147

ISSN
0925-2738
DOI
10.1007/s10858-014-9812-8
URI
http://hdl.handle.net/10203/189833
Appears in Collection
CH-Journal Papers(저널논문)
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