Alan F. Williams and A. Neil Barclay MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, Oxford OXl 3R United Kingdom E, ENCOUNTERING THE Ig SUPERFAMILY When Ig chains were first sequenced, segments within the constant regions of H and L chains showed sequence similarities, and this led to the idea that the Ig chains had all evolved from a primordial gene coding for about 100 amino acids (1). The domains within the Ig chains all contained a characteristic intrachain disulfide bond, and the idea of the domain as an independent structural unit was proposed (2). The domain hypothesis was firmly established when the structures ofV and C domains were determined to reveal a common fold forming a sandwich of two p-sheets that was stabilized by the conserved disulfide bond (3, 4). Beta-2 microglobulin (P2-m), identified in the urine of patients with kidney disease, was the first nonimmunoglobulin structure found to share sequence similarities with Ig-domains. The pz-m sequence looked like an Ig C-domain (5, 6). P2-m was subsequently discovered to be part of the major histocompatibility complex (MH C) class I structure, and sequencing of the class I heavy chain showed that a
Annual Review of Immunology – Annual Reviews
Published: Apr 1, 1988
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