The Immunoglobulin Superfamily—Domains for Cell Surface Recognition

The Immunoglobulin Superfamily—Domains for Cell Surface Recognition 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Immunology Annual Reviews

The Immunoglobulin Superfamily—Domains for Cell Surface Recognition

Annual Review of Immunology, Volume 6 (1) – Apr 1, 1988

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Publisher
Annual Reviews
Copyright
Copyright 1988 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0732-0582
eISSN
1545-3278
DOI
10.1146/annurev.iy.06.040188.002121
pmid
3289571
Publisher site
See Article on Publisher Site

Abstract

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

Journal

Annual Review of ImmunologyAnnual Reviews

Published: Apr 1, 1988

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