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2B8A

High Resolution Structure of the HDGF PWWP Domain

Summary for 2B8A
Entry DOI10.2210/pdb2b8a/pdb
DescriptorHepatoma-derived growth factor (1 entity in total)
Functional Keywordspwwp, hdgf, hormone-growth factor complex, hormone/growth factor
Biological sourceRattus norvegicus (Norway rat)
Cellular locationCytoplasm (By similarity): Q8VHK7
Total number of polymer chains1
Total formula weight12643.30
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 citationLukasik, 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: 16384999
DOI: 10.1110/ps.051751706
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237735

数据于2025-06-18公开中

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