Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 1177-1183 |
| Journal | Biophysical Journal |
| Volume | 83 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2002 |
| MoE publication type | A1 Journal article-refereed |
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Quaternary structure built from subunits combining NMR and small-angle X-ray scattering data. / Mattinen, Maija-Liisa; Pääkkönen, Kimmo; Ikonen, Teemu; Craven, Jeremy; Drakenberg, Torbjörn; Serimaa, Ritva; Waltho, Jonathan; Annila, Arto (Corresponding Author).
In: Biophysical Journal, Vol. 83, No. 2, 2002, p. 1177-1183.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Quaternary structure built from subunits combining NMR and small-angle X-ray scattering data
AU - Mattinen, Maija-Liisa
AU - Pääkkönen, Kimmo
AU - Ikonen, Teemu
AU - Craven, Jeremy
AU - Drakenberg, Torbjörn
AU - Serimaa, Ritva
AU - Waltho, Jonathan
AU - Annila, Arto
PY - 2002
Y1 - 2002
N2 - A new principle in constructing molecular complexes from the known high-resolution domain structures joining data from NMR and small-angle x-ray scattering (SAXS) measurements is described. Structure of calmodulin in complex with trifluoperazine was built from N- and C-terminal domains oriented based on residual dipolar couplings measured by NMR in a dilute liquid crystal, and the overall shape of the complex was derived from SAXS data. The residual dipolar coupling data serves to reduce angular degrees of freedom, and the small-angle scattering data serves to confine the translational degrees of freedom. The complex built by this method was found to be consistent with the known crystal structure. The study demonstrates how approximate tertiary structures of modular proteins or quaternary structures composed of subunits can be assembled from high-resolution structures of domains or subunits using mutually complementary NMR and SAXS data.
AB - A new principle in constructing molecular complexes from the known high-resolution domain structures joining data from NMR and small-angle x-ray scattering (SAXS) measurements is described. Structure of calmodulin in complex with trifluoperazine was built from N- and C-terminal domains oriented based on residual dipolar couplings measured by NMR in a dilute liquid crystal, and the overall shape of the complex was derived from SAXS data. The residual dipolar coupling data serves to reduce angular degrees of freedom, and the small-angle scattering data serves to confine the translational degrees of freedom. The complex built by this method was found to be consistent with the known crystal structure. The study demonstrates how approximate tertiary structures of modular proteins or quaternary structures composed of subunits can be assembled from high-resolution structures of domains or subunits using mutually complementary NMR and SAXS data.
U2 - 10.1016/S0006-3495(02)75241-7
DO - 10.1016/S0006-3495(02)75241-7
M3 - Article
VL - 83
SP - 1177
EP - 1183
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 2
ER -