Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix

M Sugawara, Sara Whittaker, S Bishop, L Ball, Michael Overduin

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    3 Citations (Scopus)


    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 H-1, C-13 and N-15 resonance assignments of a 20 kDa construct comprising the uniformly C-13 and N-15 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 H-1, C-13 and N-15 chemical shifts have been deposited in BMRB with accession number of 16195.
    Original languageEnglish
    Pages (from-to)215-218
    Number of pages4
    JournalBiomolecular NMR Assignments
    Issue number2
    Publication statusPublished - 1 Dec 2009


    • Lbc
    • Brx
    • PH domain
    • AKAP13
    • NMR resonance assignment


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