ArticleProtein science : a publication of the Protein Society2019
Crystal structure of the LUFS domain of human single-stranded DNA binding Protein 2 (SSBP2).
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Rewiring of LEUNIG_HOMOLOG interaction networks marks regulatory shifts from meristem to organ growth in Arabidopsis flowers.The Plant journal : for cell and molecular biology · 2025Article
- Single-stranded DNA-binding proteins are essential components of the architectural LDB1 protein complex.Molecular cell · 2025Article
- Xenopus Ssbp2 is required for embryonic pronephros morphogenesis and terminal differentiation.Scientific reports · 2023Article
- The CRL4The EMBO journal · 2021Article
- The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020Review
- Crystal structure of human LDB1 in complex with SSBP2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The LUFS domain, its transcriptional regulator proteins, and drug resistance in the fungal pathogen Candida auris.Protein science : a publication of the Protein Society · 2019Article
- Rotational symmetry of the structured Chip/LDB-SSDP core module of the Wnt enhanceosome.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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5 authors.
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Abstract
The human single-stranded DNA binding Protein 2 (SSBP2) is a tumor suppressor implicated in multiple cancer forms. The SSBP2 and related SSBP3/SSBP4 proteins are predicted to be intrinsically disordered excepted for their highly conserved N-terminal LUFS (LUG/LUH, Flo8, and SSBP/SSDP) domain. LUFS domains are found in a number of proteins including some transcriptional co-repressors. Although LUFS domains contain an N-terminal Lis homology (LisH) motif that typically forms a stable dimer, no 3D structure of any LUFS domain is available. Here, we report a crystal structure of the LUFS domain of human SSBP2 at 1.52 Å resolution. We show that the SSBP2 LUFS domain forms a homo-tetramer and reveal how an alpha-helix C-terminal to the LisH motif mediates SSBP2 tetramerization (dimerization of dimers). Conservation of the tetramerization interface among LUFS domains suggests that other LUFS domains may also form tetramers in similar manners.
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