RESUMO
The human AKAP13 protein contains DH and PH domains, which are responsible for its cell transforming activity. Despite its biomedical importance, the contribution of the PH domain to AKAP13 activity remains unclear and no three dimensional structure is available to date. Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments of a 20 kDa construct comprising the uniformly (13)C and( 15)N labeled AKAP13-PH domain and an associated helix from the DH domain which is required for its stable expression. Resonance assignment has been achieved using conventional triple resonance experiments; 95% of all back bone resonances and more than 90% of side chain resonances have been successfully assigned. The (1)H, (13)C and (15)N chemical shifts have been deposited in BMRB with accession number of 16195.
Assuntos
Proteínas de Ancoragem à Quinase A/química , Proteínas Sanguíneas/química , Proteínas de Ligação a DNA/química , Fosfoproteínas/química , Proteínas Proto-Oncogênicas/química , Fatores de Transcrição/química , Sequência de Aminoácidos , Humanos , Antígenos de Histocompatibilidade Menor , Dados de Sequência Molecular , Ressonância Magnética Nuclear Biomolecular , Estabilidade Proteica , Estrutura Secundária de Proteína , Estrutura Terciária de ProteínaRESUMO
We have assigned 1H, 13C and 15N resonances of the Bright/ARID DNA-binding domain from the human JARID1C protein, a newly discovered histone demethylase belonging to the JmjC domain-containing protein family.
