crystal structure of SSB and ssDNA complex from homo sapienscrystal structure of SSB and ssDNA complex from homo sapiens

Structural highlights

5d8f is a 3 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.35Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SOSB1_HUMAN Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways.[1] [2] [3]

See Also

References

  1. Richard DJ, Bolderson E, Cubeddu L, Wadsworth RI, Savage K, Sharma GG, Nicolette ML, Tsvetanov S, McIlwraith MJ, Pandita RK, Takeda S, Hay RT, Gautier J, West SC, Paull TT, Pandita TK, White MF, Khanna KK. Single-stranded DNA-binding protein hSSB1 is critical for genomic stability. Nature. 2008 May 29;453(7195):677-81. doi: 10.1038/nature06883. Epub 2008 Apr 30. PMID:18449195 doi:http://dx.doi.org/10.1038/nature06883
  2. Li Y, Bolderson E, Kumar R, Muniandy PA, Xue Y, Richard DJ, Seidman M, Pandita TK, Khanna KK, Wang W. HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response. J Biol Chem. 2009 Aug 28;284(35):23525-31. doi: 10.1074/jbc.C109.039586. Epub, 2009 Jul 14. PMID:19605351 doi:http://dx.doi.org/10.1074/jbc.C109.039586
  3. Huang J, Gong Z, Ghosal G, Chen J. SOSS complexes participate in the maintenance of genomic stability. Mol Cell. 2009 Aug 14;35(3):384-93. doi: 10.1016/j.molcel.2009.06.011. PMID:19683501 doi:http://dx.doi.org/10.1016/j.molcel.2009.06.011

5d8f, resolution 2.35Å

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