2M9M
Solution Structure of ERCC4 domain of human FAAP24
Summary for 2M9M
| Entry DOI | 10.2210/pdb2m9m/pdb |
| Related | 2M9N |
| NMR Information | BMRB: 19302 |
| Descriptor | Fanconi anemia-associated protein of 24 kDa (1 entity in total) |
| Functional Keywords | fanconi anemia, faap24, ercc4 domain, dna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q9BTP7 |
| Total number of polymer chains | 1 |
| Total formula weight | 16751.34 |
| Authors | |
| Primary citation | Wang, Y.,Han, X.,Wu, F.,Leung, J.W.,Lowery, M.G.,Do, H.,Chen, J.,Shi, C.,Tian, C.,Li, L.,Gong, W. Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response. Cell Res., 23:1215-1228, 2013 Cited by PubMed Abstract: The FANCM/FAAP24 heterodimer has distinct functions in protecting cells from complex DNA lesions such as interstrand crosslinks. These functions rely on the biochemical activity of FANCM/FAAP24 to recognize and bind to damaged DNA or stalled replication forks. However, the DNA-binding activity of this complex was not clearly defined. We investigated how FAAP24 contributes to the DNA-interacting functions of the FANCM/FAAP24 complex by acquiring the N-terminal and C-terminal solution structures of human FAAP24. Modeling of the FAAP24 structure indicates that FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). Testing of various FAAP24 mutations in vitro and in vivo validated this prediction derived from structural analyses. We found that the DNA-binding and FANCM-interacting functions of FAAP24, although both require the C-terminal (HhH)2 domain, can be distinguished by segregation-of-function mutations. These results demonstrate dual roles of FAAP24 in DNA damage response against crosslinking lesions, one through the formation of FANCM/FAAP24 heterodimer and the other via its ssDNA-binding activity required in optimized checkpoint activation. PubMed: 23999858DOI: 10.1038/cr.2013.124 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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