Journal article

Crystal structure of a glycosylated Fab from an IgM cryoglobulin with properties of a natural proteolytic antibody

PA Ramsland, SS Terzyan, G Cloud, CR Bourne, W Farrugia, G Tribbick, HM Geysen, CR Moomaw, CA Slaughter, AB Edmundson

BIOCHEMICAL JOURNAL | PORTLAND PRESS LTD | Published : 2006

Abstract

The 2.6 A (1 A=0.1 nm) resolution structure has been determined for the glycosylated Fab (fragment antigen binding) of an IgM (Yvo) obtained from a subject with Waldenström's macroglobulinaemia. Dynamic light scattering was used to estimate the gel point and monitor the formation of an ordered hydroscopic gel of Yvo IgM upon cooling. If a cryoglobulin forms gels in peripheral tissues and organs, the associated swelling and damage to microvasculature can result in considerable morbidity and mortality. The three-dimensional structure of the branched N-linked oligosaccharide associated with the CH1 domain (first constant domain of heavy chain) is reported. The carbohydrate may act to shield par..

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University of Melbourne Researchers