ArticleBiochemistry and biophysics reports2017
Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering.
Article in Biochemistry and biophysics reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- The solution structure of the unbound IgG Fc receptor CD64 resembles its crystal structure: Implications for function.PloS one · 2023Article
- Overall structure of fully assembled cyanobacterial KaiABC circadian clock complex by an integrated experimental-computational approach.Communications biology · 2022Article
- Biophysical characterization of dynamic structures of immunoglobulin G.Biophysical reviews · 2020Review
- Examining Membrane Proteins by Neutron Scattering.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The Fab portion of immunoglobulin G contributes to its binding to Fcγ receptor III.Scientific reports · 2019Article
- CmAbs · 2019Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A recently developed integrative approach combining varied types of experimental data has been successfully applied to three-dimensional modelling of larger biomacromolecular complexes. Deuteration-assisted small-angle neutron scattering (SANS) plays a unique role in this approach by making it possible to observe selected components in the complex. It enables integrative modelling of biomolecular complexes based on building-block structures typically provided by X-ray crystallography. In this integrative approach, it is important to be aware of the flexible properties of the individual building blocks. Here we examine the ability of SANS to detect a subtle conformational change of a multidomain protein using the Fc portion of human immunoglobulin G (IgG) interacting with a soluble form of the low-affinity Fcγ receptor IIIb (sFcγRIIIb) as a model system. The IgG-Fc glycoprotein was subjected to SANS in the absence and presence of 75%-deuterated sFcγRIIIb, which was matched out in D
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Registered trials
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