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2M9N

Solution Structure of (HhH)2 domain of human FAAP24

Summary for 2M9N
Entry DOI10.2210/pdb2m9n/pdb
Related2M9M
NMR InformationBMRB: 19303
DescriptorFanconi anemia-associated protein of 24 kDa (1 entity in total)
Functional Keywordsfanconi anemia, faap24, (hhh)2 domain, dna binding protein
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q9BTP7
Total number of polymer chains1
Total formula weight6772.76
Authors
Wu, F.,Han, X.,Shi, C.,Gong, W.,Tian, C. (deposition date: 2013-06-18, release date: 2013-09-18, Last modification date: 2024-05-15)
Primary citationWang, 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: 23999858
DOI: 10.1038/cr.2013.124
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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