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Overview

The PWWP domain belongs to the Royal family, which consists of Tudor, chromodomain, MBT(Malignant Brain Tumor), and PWWP domains. It was first identified as a structural motif includes 100 to 130 amino acids in WHSC1 protein. The name PWWP comes after its very conservative sequence, Pro-Trp-Trp-Pro located at its β2 region.^[1] This domain is mainly related to the recognition of methylated histone tail lysine and related to the epigenetic regulation of genes.

Function

The PWWP domain is also used for protein-protein interaction. This domain also may have nonspecific interaction with a DNA strand, using its abundant lysine and arginine residues.

Structure

Two disticntive The first proline affects the stability and aggregation of the protein. The proline gives more stability and oligomerization to the protein, compared to the alanine at the same position.^[2] It has two distinctive substructural motifs: β-barrel at the N-terminal region and helixes at C-terminal region.^[3] The β-barrel is very conservative feature of PWWP domains and it is composed of 5 β-strands. 3pfs has 3 helixes which are little more than many of its relatives. The stability of domain comes from both inter-substructure and intra-substructure interactions including hydrogen bonds and polar interactions. 11K 12R

Evolutionary conservations

PWWP domain is only found in eukaryotes, from a yeast to a human. The number of PWWP containing protein is also varying on species; the human has 20. The loyal family has a common structural characteristic, three conserved β-strands.^[4] The PWWP domain is also believed to be evolved from a common ancestor which had 3 β-strands. The most conservative section is the PWWP sequence, which it is named after.

Therapheutic features

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