Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium.

Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
BMC Biol 20(1):176 (2022 Aug 9)
PMID: 35945584
doi: 10.1186/s12915-022-01381-5
Submitted to SASBDB: 2022 Jan 10
Published in SASBDB:

SASDNX3 – Calcium-bound Calmodulin, including structural models

Calmodulin-1 experimental SAS data
Calcium-bound Calmodulin, including structural models Rg histogram
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
RgGuinier 2.2 nm
Dmax 7.2 nm
VolumePorod 33 nm3

SASDNY3 – Calcium-bound Calmodulin complexed with Calmidazolium

Calmodulin-1Calmidazolium experimental SAS data
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Calmidazolium monomer, 1 kDa
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
RgGuinier 1.7 nm
Dmax 5.2 nm
VolumePorod 30 nm3