Three-dimensional structure of a human immunoglobulin with a hinge deletion. | Zendy

Luke W. Guddat | Zendy; James N. Herron | Zendy; Allen B. Edmundson | Zendy

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Three-dimensional structure of a human immunoglobulin with a hinge deletion.

Author(s) -

Luke W. Guddat,

James N. Herron,

Allen B. Edmundson

Publication year - 1993

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.90.9.4271

Subject(s) - immunoglobulin fc fragments , fragment crystallizable region , immunoglobulin fab fragments , immunoglobulin light chain , chemistry , immunoglobulin domain , antibody , steric effects , cleavage (geology) , hinge , immunoglobulin g , binding site , disulfide bond , molecule , crystallography , stereochemistry , biophysics , microbiology and biotechnology , receptor , biology , biochemistry , immunology , physics , paleontology , organic chemistry , classical mechanics , fracture (geology) , complementarity determining region

X-ray analysis at 3.2-A resolution revealed that the Mcg IgG1 (lambda chain) immunoglobulin is a compact T-shaped molecule. Because of the hinge deletion, the Fc fragment lobe is pulled tightly upward into the junction of the Fab arms. Along the molecular twofold axis, the Fab arms are joined by an interchain disulfide bond between the two light chains. The antigen combining sites consist of large irregular cavities at the tips of the Fab regions. Potential complement (C1q) binding sites on Fc are sterically shielded by the Fab arms, but putative attachment sites are accessible for docking with the FcRI receptor on human monocytes and with protein A of Staphylococcus aureus.

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