Differences in the transactivation domains of p53 family members: a computational study
<p>Abstract</p> <p>The N terminal transactivation domain of p53 is regulated by ligases and coactivator proteins. The functional conformation of this region appears to be an alpha helix which is necessary for its appropriate interactions with several proteins including MDM2 and p30...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2010-02-01
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| Series: | BMC Genomics |
| _version_ | 1819038621440671744 |
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| author | Beuerman Roger W Madhumalar Arumugam Mavinahalli Jagadeesh N Lane David P Verma Chandra |
| author_facet | Beuerman Roger W Madhumalar Arumugam Mavinahalli Jagadeesh N Lane David P Verma Chandra |
| author_sort | Beuerman Roger W |
| collection | DOAJ |
| description | <p>Abstract</p> <p>The N terminal transactivation domain of p53 is regulated by ligases and coactivator proteins. The functional conformation of this region appears to be an alpha helix which is necessary for its appropriate interactions with several proteins including MDM2 and p300. Folding simulation studies have been carried out to examine the propensity and stability of this region and are used to understand the differences between the family members with the ease of helix formation following the order p53 > p73 > p63. It is clear that hydrophobic clusters control the kinetics of helix formation, while electrostatic interactions control the thermodynamic stability of the helix. Differences in these interactions between the family members may partially account for the differential binding to, and regulation by, MDM2 (and MDMX). Phosphorylations of the peptides further modulate the stability of the helix and control associations with partner proteins.</p> |
| first_indexed | 2024-12-21T08:40:13Z |
| format | Article |
| id | doaj.art-df4126c675c344b499b0b8e99b19828b |
| institution | Directory Open Access Journal |
| issn | 1471-2164 |
| language | English |
| last_indexed | 2024-12-21T08:40:13Z |
| publishDate | 2010-02-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Genomics |
| spelling | doaj.art-df4126c675c344b499b0b8e99b19828b2022-12-21T19:09:58ZengBMCBMC Genomics1471-21642010-02-0111Suppl 1S510.1186/1471-2164-11-S1-S5Differences in the transactivation domains of p53 family members: a computational studyBeuerman Roger WMadhumalar ArumugamMavinahalli Jagadeesh NLane David PVerma Chandra<p>Abstract</p> <p>The N terminal transactivation domain of p53 is regulated by ligases and coactivator proteins. The functional conformation of this region appears to be an alpha helix which is necessary for its appropriate interactions with several proteins including MDM2 and p300. Folding simulation studies have been carried out to examine the propensity and stability of this region and are used to understand the differences between the family members with the ease of helix formation following the order p53 > p73 > p63. It is clear that hydrophobic clusters control the kinetics of helix formation, while electrostatic interactions control the thermodynamic stability of the helix. Differences in these interactions between the family members may partially account for the differential binding to, and regulation by, MDM2 (and MDMX). Phosphorylations of the peptides further modulate the stability of the helix and control associations with partner proteins.</p> |
| spellingShingle | Beuerman Roger W Madhumalar Arumugam Mavinahalli Jagadeesh N Lane David P Verma Chandra Differences in the transactivation domains of p53 family members: a computational study BMC Genomics |
| title | Differences in the transactivation domains of p53 family members: a computational study |
| title_full | Differences in the transactivation domains of p53 family members: a computational study |
| title_fullStr | Differences in the transactivation domains of p53 family members: a computational study |
| title_full_unstemmed | Differences in the transactivation domains of p53 family members: a computational study |
| title_short | Differences in the transactivation domains of p53 family members: a computational study |
| title_sort | differences in the transactivation domains of p53 family members a computational study |
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