Structural variation in PWWP domains.

Leanne M Slater; Mark D Allen; Mark Bycroft

doi:10.1016/s0022-2836(03)00470-4

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Structural variation in PWWP domains.

Leanne M Slater·Mark D Allen·Mark Bycroft

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Abstract

The PWWP domain is a ubiquitous eukaryotic protein module characterised by a region of sequence similarity of approximately 80 amino acids containing a highly conserved PWWP motif. It is frequently found in proteins associated with chromatin. We have determined the structure of a PWWP domain from the S. pombe protein SPBC215.07c using NMR spectroscopy. The structure is composed of a five stranded beta barrel followed by two alpha helices. Comparison to the recently reported structure of a homologous domain from the mammalian DNA methyltransferase Dnmt3b reveals substantial differences both in the C-terminal helical region and in the PWWP motif.

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Amino Acid Sequence Conserved Sequence DNA (Cytosine-5-)-Methyltransferases Hydrophobic and Hydrophilic Interactions Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Tertiary Schizosaccharomyces pombe Proteins Sequence Homology, Amino Acid Structural Homology, Protein DNA Methyltransferase 3B Journal Article

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Leanne M Slater, Mark D Allen, Mark Bycroft. 2003-07-11. Structural variation in PWWP domains.. https://doi.org/10.1016/s0022-2836(03)00470-4

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