Ontology highlight
ABSTRACT:
SUBMITTER: Heering J
PROVIDER: S-EPMC4815341 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Heering Jan J Jonker Hendrik R A HR Löhr Frank F Schwalbe Harald H Dötsch Volker V
Protein science : a publication of the Protein Society 20151125 2
Most members of the p53 family of transcription factors form tetramers. Responsible for determining the oligomeric state is a short oligomerization domain consisting of one β-strand and one α-helix. With the exception of human p53 all other family members investigated so far contain a second α-helix as part of their tetramerization domain. Here we have used nuclear magnetic resonance spectroscopy to characterize the oligomerization domains of the two p53-like proteins from the tunicate Ciona int ...[more]