Evidence against a dimeric structure for membrane-bound HLA antigens.

Human histocompatbility (HLA) antigens are expressed on the surfaces of almost all cell types and according to various criteria are integral membrane glycoproteins. They are composed of equimolar amounts of two dissimilar polypeptide chains which are non covalently linked and which have molecular we...

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Main Authors: Snary, D, Goodfellow, P, Bodmer, W, Crumpton, M
Format: Journal article
Language:English
Published: 1975
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author Snary, D
Goodfellow, P
Bodmer, W
Crumpton, M
author_facet Snary, D
Goodfellow, P
Bodmer, W
Crumpton, M
author_sort Snary, D
collection OXFORD
description Human histocompatbility (HLA) antigens are expressed on the surfaces of almost all cell types and according to various criteria are integral membrane glycoproteins. They are composed of equimolar amounts of two dissimilar polypeptide chains which are non covalently linked and which have molecular weights of about 43,000 and 12,000 as judged by polyacrylamide gel electrophoresis in sodium dodecyl sulphate (SDS). The larger chain carries the polymorphic allogeneic specificities and all of the carbohydrate. The smaller chain represents β2 microglobulin, whose amino acid sequence shows marked homology to the C(H)3 domain of the γ 1 chain of immunoglobulin G. This homology and other arguments have led to the proposals that HLA antigens and immunoglobulins have a common evolutionary origin, and that HLA antigens have an immunoglobulin like structure in which two basic units of one each of the larger and smaller polypeptide chains are linked either non covalently by a disulphide bridge to give a 4 chain dimer of molecular weight 110,000. In contrast to the latter proposal, some results presented here suggest that HLA antigens do not have a dimeric structure.
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spelling oxford-uuid:888da4c9-5a11-463c-8802-1df879b04d002022-03-26T22:18:06ZEvidence against a dimeric structure for membrane-bound HLA antigens.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:888da4c9-5a11-463c-8802-1df879b04d00EnglishSymplectic Elements at Oxford1975Snary, DGoodfellow, PBodmer, WCrumpton, MHuman histocompatbility (HLA) antigens are expressed on the surfaces of almost all cell types and according to various criteria are integral membrane glycoproteins. They are composed of equimolar amounts of two dissimilar polypeptide chains which are non covalently linked and which have molecular weights of about 43,000 and 12,000 as judged by polyacrylamide gel electrophoresis in sodium dodecyl sulphate (SDS). The larger chain carries the polymorphic allogeneic specificities and all of the carbohydrate. The smaller chain represents β2 microglobulin, whose amino acid sequence shows marked homology to the C(H)3 domain of the γ 1 chain of immunoglobulin G. This homology and other arguments have led to the proposals that HLA antigens and immunoglobulins have a common evolutionary origin, and that HLA antigens have an immunoglobulin like structure in which two basic units of one each of the larger and smaller polypeptide chains are linked either non covalently by a disulphide bridge to give a 4 chain dimer of molecular weight 110,000. In contrast to the latter proposal, some results presented here suggest that HLA antigens do not have a dimeric structure.
spellingShingle Snary, D
Goodfellow, P
Bodmer, W
Crumpton, M
Evidence against a dimeric structure for membrane-bound HLA antigens.
title Evidence against a dimeric structure for membrane-bound HLA antigens.
title_full Evidence against a dimeric structure for membrane-bound HLA antigens.
title_fullStr Evidence against a dimeric structure for membrane-bound HLA antigens.
title_full_unstemmed Evidence against a dimeric structure for membrane-bound HLA antigens.
title_short Evidence against a dimeric structure for membrane-bound HLA antigens.
title_sort evidence against a dimeric structure for membrane bound hla antigens
work_keys_str_mv AT snaryd evidenceagainstadimericstructureformembraneboundhlaantigens
AT goodfellowp evidenceagainstadimericstructureformembraneboundhlaantigens
AT bodmerw evidenceagainstadimericstructureformembraneboundhlaantigens
AT crumptonm evidenceagainstadimericstructureformembraneboundhlaantigens