Conformational stability and activity of p73 require a second helix in the tetramerization domain.

Coutandin, D; Löhr, F; Niesen, FH; Ikeya, T; Weber, TA; Schäfer, B; Zielonka, EM; Bullock, AN; Yang, A; Güntert, P; Knapp, S; McKeon, F; Ou, HD; Dötsch, V

Abstract:

p73 and p63, the two ancestral members of the p53 family, are involved in neurogenesis, epithelial stem cell maintenance and quality control of female germ cells. The highly conserved oligomerization domain (OD) of tumor suppressor p53 is essential for its biological functions, and its structure was believed to be the prototype for all three proteins. However, we report that the ODs of p73 and p63 differ from the OD of p53 by containing an additional alpha-helix that is not present in the str...

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APA Style

Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Zielonka, E. M., Bullock, A. N., Yang, A., Güntert, P., Knapp, S., McKeon, F., Ou, H. D., & Dötsch, V. (2009). Conformational stability and activity of p73 require a second helix in the tetramerization domain. Cell Death and Differentiation, 16(12), 1582–1589.

MLA Style

Coutandin, D., et al. “Conformational Stability and Activity of p73 Require a Second Helix in the Tetramerization Domain.” Cell Death and Differentiation, vol. 16, no. 12, 2009, pp. 1582–89.

Chicago Style

Coutandin, D, F Löhr, FH Niesen, T Ikeya, TA Weber, B Schäfer, EM Zielonka, et al. 2009. “Conformational Stability and Activity of p73 Require a Second Helix in the Tetramerization Domain.” Cell Death and Differentiation 16 (12): 1582–89.
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