Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids.

Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
Biophys J 115(7):1231-1239 (2018 Oct 2)
PMID: 30197181
doi: 10.1016/j.bpj.2018.07.039 		Submitted to SASBDB: 2018 Jul 3
Published in SASBDB:

SASDDJ9 – Conformation of the R1-3 human dystrophin fragment (SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7
RgGuinier 4.2 nm
Dmax 17.7 nm
VolumePorod 46 nm3

SASDDK9 – Conformation of R1-3 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

R1-3 human dystrophin fragment experimental SAS data
DAMMIF model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7
RgGuinier 4.1 nm
Dmax 17.8 nm
VolumePorod 50 nm3

SASDDL9 – Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7
RgGuinier 6.2 nm
Dmax 24.8 nm
VolumePorod 100 nm3