Clarification of solution structure and its modulation in proteins and protein complexes is
crucially important to understand dynamical ordering in macromolecular systems. Small …

Immunoglobulin G (IgG) is a major antibody and functions as a hub linking specific antigen
binding and recruitment of effector molecules typified by Fcγ receptors (FcγRs). These …

Most cells active in the immune system express receptors for antibodies which mediate a
variety of defensive mechanisms. These receptors interact with the Fc portion of the antibody …

FcγRI (CD64) is the only high-affinity Fcγ receptor found on monocytes, macrophages,
eosinophils, neutrophils and dendritic cells. It binds immunoglobulin G (IgG) antibody …

In the cyanobacterial circadian clock system, KaiA, KaiB and KaiC periodically assemble
into a large complex. Here we determined the overall structure of their fully assembled …

Immunoglobulin G (IgG) is a major serum glycoprotein that exerts the role of antibody in the
immune system. This multifunctional glycoprotein couples antigen recognition with a variety …

Euryarchaeal genomes encode proteasome-assembling chaperone homologs, PbaA and
PbaB, although archaeal proteasome formation is a chaperone-independent process …

This study employed high-speed atomic force microscopy to quantitatively analyze the
interactions between therapeutic antibodies and Fcγ receptors (FcγRs). Antibodies are …

The N-linked glycan in immunoglobulin G is critical for the stability and function of the
crystallizable fragment (Fc) region. Alteration of these protein properties upon the removal of …

Small-angle neutron scattering (SANS) and small-angle X-ray scattering (SAXS) are
powerful techniques for the structural characterization of biomolecular complexes. In …