Sandbox Reserved 897: Difference between revisions
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== Structure == | == Structure == | ||
The main characteristic of PWWP domains is the two distinctive substructural motifs: β-barrel at the N-terminal region and helixes at C-terminal 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 β-barrel is a very conservative feature of PWWP domains and the one at 3pfs is composed of 5 β-strands. The helixes at the C-terminal region are very different and 3pfs has 3 helixes which are little more than many of its relatives. The Pro-Trp-Trp-Pro motif, which is the most conservative, is little different in 3pfs, just like its closely-related proteins. The PWWP domains in BRPF family are composed of Tyr-Pro-Ser-Tyr and may suggest they would have a similar affinity. The stability of domain comes from both inter-substructure and intra-substructure interactions including hydrogen bonds and polar interactions. One unique feature of PWWP motif is that the first position 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.<ref>Hung YL, Lee HJ, Jiang I, Lin SC, Lo WC, Lin YJ, Sue SC. The first residue of the PWWP motif modulates HATH domain binding, Stability, and Protein–Protein Interaction. Biochemistry. 2015 Jul 7;54(26):4063-74.</ref> | The main characteristic of PWWP domains is the two distinctive substructural motifs: β-barrel at the N-terminal region and helixes at C-terminal 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 β-barrel is a very conservative feature of PWWP domains and the one at 3pfs is composed of 5 β-strands. The helixes at the C-terminal region are very different and 3pfs has 3 helixes which are little more than many of its relatives. The Pro-Trp-Trp-Pro motif, which is the most conservative, is little different in 3pfs, just like its closely-related proteins. The PWWP domains in BRPF family are composed of Tyr-Pro-Ser-Tyr and may suggest they would have a similar affinity. The stability of domain comes from both inter-substructure and intra-substructure interactions including hydrogen bonds and polar interactions. One unique feature of PWWP motif is that the first position 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.<ref>Hung YL, Lee HJ, Jiang I, Lin SC, Lo WC, Lin YJ, Sue SC. The first residue of the PWWP motif modulates HATH domain binding, Stability, and Protein–Protein Interaction. Biochemistry. 2015 Jul 7;54(26):4063-74.</ref> | ||
[[Image:3pfs cartoon.png|thumb|center|512 px| '''Figure | [[Image:3pfs cartoon.png|thumb|center|512 px| '''Figure 1A:''' Cartoon model of 3PFS motif. β-sheets(magenta) and helixes(orange) are shown. generated in PyMOL using PDB: ''3PFS'']] | ||
[[Image:3pfs alignment.png|thumb|center|512 px| '''Figure 1B:''' The alignment of BRPF2 PWWP domain and BRPF3 PWWP domain. The green box indicates the 'PWWP' motif. generated in Tcoffee using PDB: ''3PFS', '2X35'']] | |||
== Function == | == Function == | ||
