2RRD

Structure of HRDC domain from human Bloom syndrome protein, BLM

2RRD の概要

• エントリーDOI: 10.2210/pdb2rrd/pdb
• NMR情報: BMRB: 11252
• 分子名称: HRDC domain from Bloom syndrome protein (1 entity in total)
• 機能のキーワード: dna helicase, recq family, bloom syndrome protein, hrdc domain, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P54132
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11281.92

構造登録者

Sato, A.,Mishima, M.,Nagai, A.,Kim, S.Y.,Ito, Y.,Hakoshima, T.,Jee, J.G.,Kitano, K. (登録日: 2010-07-19, 公開日: 2010-09-08, 最終更新日: 2024-05-01)

主引用文献

Sato, A.,Mishima, M.,Nagai, A.,Kim, S.Y.,Ito, Y.,Hakoshima, T.,Jee, J.G.,Kitano, K.
Solution structure of the HRDC domain of human Bloom syndrome protein BLM
J.Biochem., 148:517-525, 2010

PubMed Abstract: Bloom syndrome is a rare genetic disorder characterized by severe growth retardation and cancer predisposition. The disease is caused by a loss of function of the Bloom syndrome protein (BLM), a member of the RecQ family of DNA helicases. Here we report on the first 3D structure of a BLM fragment, a solution structure of the C-terminal helicase-and-ribonuclease D-C-terminal (HRDC) domain from human BLM. The structure reveals unique features of BLM HRDC that are distinct from the HRDC domain of Werner syndrome protein. In particular, BLM HRDC retains many acidic residues exposed to the solvent, which makes the domain surface extensively electronegative. Consistent with this, fluorescence polarization assays showed an inability of isolated BLM HRDC to interact with DNA substrates. Analyses employing ultracentrifugation, gel-filtration, CD spectroscopy and dynamic light scattering showed that the BLM HRDC domain exists as a stable monomer in solution. The results show that BLM HRDC is a compact, robust and acidic motif which may play a distinct role apart from DNA binding.

PubMed: 20739603
DOI: 10.1093/jb/mvq097

実験手法

SOLUTION NMR