Sandbox Reserved 897
From Proteopedia
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== Overview == | == Overview == | ||
| - | The PWWP domain belongs to the Royal family, which consists of Tudor, chromodomain, MBT, and PWWP domains. It was first identified as a structural motif includes 100 to 130 amino acids. The name PWWP comes after its very conservative sequence, Pro-Trp-Trp-Pro located at its β2 region.<ref> | + | 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. The name PWWP comes after its very conservative sequence, Pro-Trp-Trp-Pro located at its β2 region.<ref>Rona GB, Eleutherio EC, Pinheiro AS. PWWP domains and their modes of sensing DNA and histone methylated lysines. Biophysical reviews. 2016 Mar 1;8(1):63-74.</ref> The first proline affects the stability and aggregation of the protein. The PWWP domain is also used for protein-protein interaction. This domain also may have nonspecific interaction with DNA strand, using its abundant lysin and arginine residues. |
== Function == | == Function == | ||
Revision as of 23:35, 22 April 2020
| 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
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References
- ↑ Rona GB, Eleutherio EC, Pinheiro AS. PWWP domains and their modes of sensing DNA and histone methylated lysines. Biophysical reviews. 2016 Mar 1;8(1):63-74.
