2B8A
High Resolution Structure of the HDGF PWWP Domain
Summary for 2B8A
Entry DOI | 10.2210/pdb2b8a/pdb |
Descriptor | Hepatoma-derived growth factor (1 entity in total) |
Functional Keywords | pwwp, hdgf, hormone-growth factor complex, hormone/growth factor |
Biological source | Rattus norvegicus (Norway rat) |
Cellular location | Cytoplasm (By similarity): Q8VHK7 |
Total number of polymer chains | 1 |
Total formula weight | 12643.30 |
Authors | Lukasik, S.M.,Cierpicki, T.,Borloz, M.,Grembecka, J.,Everett, A.,Bushweller, J.H. (deposition date: 2005-10-06, release date: 2005-12-06, Last modification date: 2024-05-22) |
Primary citation | Lukasik, S.M.,Cierpicki, T.,Borloz, M.,Grembecka, J.,Everett, A.,Bushweller, J.H. High resolution structure of the HDGF PWWP domain: a potential DNA binding domain. Protein Sci., 15:314-323, 2006 Cited by PubMed Abstract: Hepatoma Derived Growth Factor (HDGF) is an endogenous nuclear-targeted mitogen that is linked with human disease. HDGF is a member of the weakly conserved PWWP domain family. This 70-amino acid motif, originally identified from the WHSC1 gene, has been found in more than 60 eukaryotic proteins. In addition to the PWWP domain, many proteins in this class contain known chromatin remodeling domains, suggesting a role for HDGF in chromatin remodeling. We have determined the NMR structure of the HDGF PWWP domain to high resolution using a combination of NOEs, J-couplings, and dipolar couplings. Comparison of this structure to a previously determined structure of the HDGF PWWP domain shows a significant difference in the C-terminal region. Comparison to structures of other PWWP domains shows a high degree of similarity to the PWWP domain structures from Dnmt3b and mHRP. The results of selected and amplified binding assay and NMR titrations with DNA suggest that the HDGF PWWP domain may function as a nonspecific DNA-binding domain. Based on the NMR titrations, we propose a model of the interaction of the PWWP domain with DNA. PubMed: 16384999DOI: 10.1110/ps.051751706 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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