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

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Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix. / Sugawara, M; Whittaker, Sara; Bishop, S; Ball, L; Overduin, Michael.

In: Biomolecular NMR Assignments, Vol. 3, No. 2, 01.12.2009, p. 215-218.

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Sugawara, M ; Whittaker, Sara ; Bishop, S ; Ball, L ; Overduin, Michael. / Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix. In: Biomolecular NMR Assignments. 2009 ; Vol. 3, No. 2. pp. 215-218.

Bibtex

@article{7c2d1e98e76d4346a035ebd7fbb27afa,
title = "Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix",
abstract = "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.",
keywords = "Lbc, Brx, PH domain, AKAP13, NMR resonance assignment",
author = "M Sugawara and Sara Whittaker and S Bishop and L Ball and Michael Overduin",
year = "2009",
month = dec
day = "1",
doi = "10.1007/s12104-009-9178-0",
language = "English",
volume = "3",
pages = "215--218",
journal = "Biomolecular NMR Assignments",
issn = "1874-2718",
publisher = "Springer",
number = "2",

}

RIS

TY - JOUR

T1 - Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix

AU - Sugawara, M

AU - Whittaker, Sara

AU - Bishop, S

AU - Ball, L

AU - Overduin, Michael

PY - 2009/12/1

Y1 - 2009/12/1

N2 - 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.

AB - 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.

KW - Lbc

KW - Brx

KW - PH domain

KW - AKAP13

KW - NMR resonance assignment

U2 - 10.1007/s12104-009-9178-0

DO - 10.1007/s12104-009-9178-0

M3 - Article

C2 - 19888694

VL - 3

SP - 215

EP - 218

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

SN - 1874-2718

IS - 2

ER -