Sandbox Reserved 897

This Sandbox is Reserved from Jan 13 through July 31, 2020 for use in the course Protein Structure in Drug Discovery taught by Karen C. Glass at the ACPHS, Colchester, United States. This reservation includes Sandbox Reserved 895 through Sandbox Reserved 901.

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BRPF3 PWWP binding domain 3PFS

spinqualitylabelsall models BRPF3 PWWP domain Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. 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. 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. 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 This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.