Solution structure of the tetrameric minimum transforming domain of p53

Weontae Lee, Timothy S. Harvey, Ya Yin, Patrick Yau, David Litchfield, Cheryl H. Arrowsmith

Research output: Contribution to journalArticle

234 Citations (Scopus)

Abstract

We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.

Original languageEnglish
Pages (from-to)877-890
Number of pages14
JournalNature Structural Biology
Volume1
Issue number12
DOIs
Publication statusPublished - 1994 Dec

Fingerprint

Phosphorylation
Dimers
Intrinsically Disordered Proteins
Oligomerization
Nuclear magnetic resonance spectroscopy
Phosphotransferases
Magnetic Resonance Spectroscopy
DNA
Proteins

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

Cite this

Lee, W., Harvey, T. S., Yin, Y., Yau, P., Litchfield, D., & Arrowsmith, C. H. (1994). Solution structure of the tetrameric minimum transforming domain of p53. Nature Structural Biology, 1(12), 877-890. https://doi.org/10.1038/nsb1294-877
Lee, Weontae ; Harvey, Timothy S. ; Yin, Ya ; Yau, Patrick ; Litchfield, David ; Arrowsmith, Cheryl H. / Solution structure of the tetrameric minimum transforming domain of p53. In: Nature Structural Biology. 1994 ; Vol. 1, No. 12. pp. 877-890.
@article{438535a504d74455911504065565c6ec,
title = "Solution structure of the tetrameric minimum transforming domain of p53",
abstract = "We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.",
author = "Weontae Lee and Harvey, {Timothy S.} and Ya Yin and Patrick Yau and David Litchfield and Arrowsmith, {Cheryl H.}",
year = "1994",
month = "12",
doi = "10.1038/nsb1294-877",
language = "English",
volume = "1",
pages = "877--890",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "12",

}

Lee, W, Harvey, TS, Yin, Y, Yau, P, Litchfield, D & Arrowsmith, CH 1994, 'Solution structure of the tetrameric minimum transforming domain of p53', Nature Structural Biology, vol. 1, no. 12, pp. 877-890. https://doi.org/10.1038/nsb1294-877

Solution structure of the tetrameric minimum transforming domain of p53. / Lee, Weontae; Harvey, Timothy S.; Yin, Ya; Yau, Patrick; Litchfield, David; Arrowsmith, Cheryl H.

In: Nature Structural Biology, Vol. 1, No. 12, 12.1994, p. 877-890.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Solution structure of the tetrameric minimum transforming domain of p53

AU - Lee, Weontae

AU - Harvey, Timothy S.

AU - Yin, Ya

AU - Yau, Patrick

AU - Litchfield, David

AU - Arrowsmith, Cheryl H.

PY - 1994/12

Y1 - 1994/12

N2 - We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.

AB - We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.

UR - http://www.scopus.com/inward/record.url?scp=84970061891&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84970061891&partnerID=8YFLogxK

U2 - 10.1038/nsb1294-877

DO - 10.1038/nsb1294-877

M3 - Article

C2 - 7773777

AN - SCOPUS:84970061891

VL - 1

SP - 877

EP - 890

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 12

ER -