A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes.

Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL
J Immunol 207(11):2856-2867 (2021 Dec 1)
PMID: 34759015
doi: 10.4049/jimmunol.2100815
Submitted to SASBDB: 2021 Jan 15
Published in SASBDB:

SASDKV7 – CCP2-SP domains of the complement C1r subcomponent

Complement C1r subcomponent experimental SAS data
PYMOL model
Sample: Complement C1r subcomponent monomer, 38 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 24
RgGuinier 2.4 nm
Dmax 7.9 nm
VolumePorod 63 nm3

SASDKW7 – Complement inhibitory domain of the Borrelia burgdorferi fibronectin-binding protein BBK32

Fibronectin-binding protein BBK32 experimental SAS data
PYMOL model
Sample: Fibronectin-binding protein BBK32 monomer, 17 kDa Borreliella burgdorferi B31 protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 24
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 34 nm3

SASDKX7 – CCP2-SP domains of the complement C1r subcomponent bound to the complement inhibitory domain of the Borrelia burgdorferi fibronectin-binding protein BBK32

Fibronectin-binding protein BBK32Complement C1r subcomponent experimental SAS data
PYMOL model
Sample: Fibronectin-binding protein BBK32 monomer, 17 kDa Borrelia burgdorferi (strain … protein
Complement C1r subcomponent monomer, 38 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 24
RgGuinier 2.8 nm
Dmax 8.6 nm
VolumePorod 75 nm3