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Structural and histone binding ability characterizations of human PWWP domains.

Wu H, Zeng H, Lam R, Tempel W, Amaya MF, Xu C, Dombrovski L, Qiu W, Wang Y, Min J
PLoS One 6 e18919 (2011)
Related entries: 3eae, 3l42, 3llr, 3lyi, 3mo8, 3pfs, 3pmi, 3qby, 3qkj

Cited: 99 times
EuropePMC logo PMID: 21720545

Abstract

Background

The PWWP domain was first identified as a structural motif of 100-130 amino acids in the WHSC1 protein and predicted to be a protein-protein interaction domain. It belongs to the Tudor domain 'Royal Family', which consists of Tudor, chromodomain, MBT and PWWP domains. While Tudor, chromodomain and MBT domains have long been known to bind methylated histones, PWWP was shown to exhibit histone binding ability only until recently.

Conclusion

PWWP proteins constitute a new family of methyl lysine histone binders. The PWWP domain consists of three motifs: a canonical β-barrel core, an insertion motif between the second and third β-strands and a C-terminal α-helix bundle. Both the canonical β-barrel core and the insertion motif are directly involved in histone binding. The PWWP domain has been previously shown to be a DNA binding domain. Therefore, the PWWP domain exhibits dual functions: binding both DNA and methyllysine histones.

Reviews - 3qj6 mentioned but not cited (1)

  1. PWWP domains and their modes of sensing DNA and histone methylated lysines. Rona GB, Eleutherio ECA, Pinheiro AS. Biophys Rev 8 63-74 (2016)

Articles - 3qj6 mentioned but not cited (2)

  1. ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression. Wen H, Li Y, Xi Y, Jiang S, Stratton S, Peng D, Tanaka K, Ren Y, Xia Z, Wu J, Li B, Barton MC, Li W, Li H, Shi X. Nature 508 263-268 (2014)
  2. Structural and histone binding ability characterizations of human PWWP domains. Wu H, Zeng H, Lam R, Tempel W, Amaya MF, Xu C, Dombrovski L, Qiu W, Wang Y, Min J. PLoS One 6 e18919 (2011)


Reviews citing this publication (28)

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Articles citing this publication (68)

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