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.
Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix.,Sugawara M, Whittaker SB, Bishop S, Ball L, Overduin M Biomol NMR Assign. 2009 Dec;3(2):215-8. Epub 2009 Jul 18. PMID:19888694[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Sugawara M, Whittaker SB, Bishop S, Ball L, Overduin M. Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix. Biomol NMR Assign. 2009 Dec;3(2):215-8. Epub 2009 Jul 18. PMID:19888694 doi:10.1007/s12104-009-9178-0
