Versatility in phospho-dependent molecular recognition of the XRCC1 and XRCC4 DNA-damage scaffolds by aprataxin-family FHA domains
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- 作者：Amy L. Cherrya ; 1 ; Timothy J. Notta ; 2 ; Geoffrey Kellyb ; Stuart L. Rultenb ; Keith W. Caldecottb ; Stephen J. Smerdona ; Steve.Smerdon@crick.ac.uk" class="auth_mail" title="E-mail the corresponding author
- 关键词：APLF ; aprataxin- and PNK-like factor ; PNKP ; polynucleotide kinase phosphatase ; FHA ; forkhead-associated ; XRCC1 ; X-ray repair cross-complementing protein 1 ; XRCC4 ; X-ray repair cross-complementing protein 4 ; PARP-1 ; poly(ADP-ribose)polymerase 1 ; NHEJ ; non-homologous end-joining ; DNA-PKcs ; catalytic subunit of DNA-dependent protein kinase ; CK2 ; casein kinase 2 ; HIT ; Histidine triad ; ZF ; zinc finger ; NTD ; N-terminal domain ; BRCT ; BRCA1 C-terminal ; CC ; coiled-coil ; ITC ; isothermal titration calorime
- 刊名：DNA Repair
- 出版年：2015
- 出版时间：November 2015
- 年：2015
- 卷：35
- 期：Complete
- 页码：116-125
- 全文大小：2656 K
文摘
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Aprataxin and APLF FHA domains show distinct specificities for XRCC4 and XRCC1.
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Specificity is modulated by multi-site phosphorylation.
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The crystal structure of APLF FHA and triphosphorylated XRCC4 peptide reveals a conserved mode of core pSpT motif binding.
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Overall phospho-dependent binding versatility of Aptx-family FHA domain proteins is provided by FHA surface basicity.