2RRD
Structure of HRDC domain from human Bloom syndrome protein, BLM
Summary for 2RRD
| Entry DOI | 10.2210/pdb2rrd/pdb |
| NMR Information | BMRB: 11252 |
| Descriptor | HRDC domain from Bloom syndrome protein (1 entity in total) |
| Functional Keywords | dna helicase, recq family, bloom syndrome protein, hrdc domain, dna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P54132 |
| Total number of polymer chains | 1 |
| Total formula weight | 11281.92 |
| Authors | Sato, A.,Mishima, M.,Nagai, A.,Kim, S.Y.,Ito, Y.,Hakoshima, T.,Jee, J.G.,Kitano, K. (deposition date: 2010-07-19, release date: 2010-09-08, Last modification date: 2024-05-01) |
| Primary citation | 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 Cited by 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: 20739603DOI: 10.1093/jb/mvq097 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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