Editing P53 (section)

== Oligomerization states ==

p53 initially forms [[protein dimer|dimers]] cotranslationally during protein synthesis on ribosomes.<ref name="Nicholls_2002">{{cite journal | vauthors = Nicholls CD, McLure KG, Shields MA, Lee PW | title = Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect | journal = The Journal of Biological Chemistry | volume = 277 | issue = 15 | pages = 12937–12945 | date = April 2002 | pmid = 11805092 | doi = 10.1074/jbc.M108815200 | doi-access = free }}</ref>  Each dimer comprises two p53 monomers linked via their oligomerization domains.<ref name="Suri_1999">{{cite journal | vauthors = Suri V, Lanjuin A, Rosbash M | title = TIMELESS-dependent positive and negative autoregulation in the Drosophila circadian clock | journal = The EMBO Journal | volume = 18 | issue = 3 | pages = 675–686 | date = February 1999 | pmid = 9927427 | pmc = 1171160 | doi = 10.1093/emboj/18.3.675 }}</ref>

Dimers further associate posttranslationally into [[tetramer]]s (a dimer of dimers).<ref name="Nicholls_2002">{{cite journal | vauthors = Nicholls CD, McLure KG, Shields MA, Lee PW | title = Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect | journal = The Journal of Biological Chemistry | volume = 277 | issue = 15 | pages = 12937–12945 | date = April 2002 | pmid = 11805092 | doi = 10.1074/jbc.M108815200 | doi-access = free }}</ref><ref name="Natan_2009">{{cite journal | vauthors = Natan E, Hirschberg D, Morgner N, Robinson CV, Fersht AR | title = Ultraslow oligomerization equilibria of p53 and its implications | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 34 | pages = 14327–14332 | date = August 2009 | pmid = 19667193 | pmc = 2731847 | doi = 10.1073/pnas.0907840106 | doi-access = free | bibcode = 2009PNAS..10614327N }}</ref> The tetramerization domain (residues 325–356) stabilizes this structure.<ref name="Natan_2009">{{cite journal | vauthors = Natan E, Hirschberg D, Morgner N, Robinson CV, Fersht AR | title = Ultraslow oligomerization equilibria of p53 and its implications | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 34 | pages = 14327–14332 | date = August 2009 | pmid = 19667193 | pmc = 2731847 | doi = 10.1073/pnas.0907840106 | doi-access = free | bibcode = 2009PNAS..10614327N }}</ref> Tetramers are the active form for DNA binding and transcriptional regulation.<ref name="Ho_2006">{{cite journal | vauthors = Ho WC, Fitzgerald MX, Marmorstein R | title = Structure of the p53 core domain dimer bound to DNA | journal = The Journal of Biological Chemistry | volume = 281 | issue = 29 | pages = 20494–20502 | date = July 2006 | pmid = 16717092 | doi = 10.1074/jbc.M603634200 | doi-access = free }}</ref><ref name="Suri_1999">{{cite journal | vauthors = Suri V, Lanjuin A, Rosbash M | title = TIMELESS-dependent positive and negative autoregulation in the Drosophila circadian clock | journal = The EMBO Journal | volume = 18 | issue = 3 | pages = 675–686 | date = February 1999 | pmid = 9927427 | pmc = 1171160 | doi = 10.1093/emboj/18.3.675 }}</ref>