Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering
| Autor: | Saeko Yanaka, Linoel Porcar, Hirokazu Yagi, Anne L. Martel, Masaaki Sugiyama, Nobuhiro Sato, Koichi Kato, Yutaro Ueki, Rintaro Inoue, Rina Yogo |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Conformational change Chemistry Biophysics Neutron scattering Biochemistry Small-angle neutron scattering Characterization (materials science) lcsh:Biochemistry 03 medical and health sciences Crystallography 030104 developmental biology Low affinity lcsh:Biology (General) lcsh:QD415-436 Deformation (engineering) Receptor Glycoprotein lcsh:QH301-705.5 Research Article |
| Zdroj: | Biochemistry and Biophysics Reports Biochemistry and Biophysics Reports, Vol 12, Iss C, Pp 1-4 (2017) |
| ISSN: | 2405-5808 |
| Popis: | 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 D2O solution. This inverse contrast-matching technique enabled selective observation of SANS from IgG-Fc, thereby detecting its subtle structural deformation induced by the receptor binding. The SANS data were successfully interpreted by considering previously reported crystallographic data and an equilibrium between free and sFcγRIIIb-bound forms. Our SANS data thus demonstrate the applicability of SANS in the integrative approach dealing with biomacromolecular complexes composed of weakly associated building blocks with conformational plasticity. Highlights • IgG-Fc glycoprotein was structurally characterized by small-angle neutron scattering. • Fc was selectively observed under equilibrium between free and receptor-bound forms. • Receptor-induced conformational change of Fc was successfully detected. |
| Databáze: | OpenAIRE |
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