THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M

An insight into the structural features of human IgM that are responsible for its capacity to bind the first component of complement (C) has been obtained by examining the ability of IgM subfragments to bind active C1 (C1). The smallest two fragments found to bind C1 were the major CNBr fragment of...

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Detalles Bibliográficos
Autores principales: Hurst, Mary M., Volanakis, John E., Hester, Raymond B., Stroud, Robert M., Bennett, J. Claude
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1974
Materias:
Brief Definitive Reports
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139640/
https://www.ncbi.nlm.nih.gov/pubmed/4427090
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author Hurst, Mary M.
Volanakis, John E.
Hester, Raymond B.
Stroud, Robert M.
Bennett, J. Claude
author_facet Hurst, Mary M.
Volanakis, John E.
Hester, Raymond B.
Stroud, Robert M.
Bennett, J. Claude
author_sort Hurst, Mary M.
collection PubMed
description An insight into the structural features of human IgM that are responsible for its capacity to bind the first component of complement (C) has been obtained by examining the ability of IgM subfragments to bind active C1 (C1). The smallest two fragments found to bind C1 were the major CNBr fragment of the Fc portion of IgM and the C(H)4 fragment of the carboxy-terminal domain. The smallest fragment which fixes C1 has a disaggregated mol wt of 6,800, consists of 60 residues, and contains no carbohydrate. Structural considerations and sequence overlaps suggest that the amino-terminal side of the C(H)4 domain (24 amino acid residues) might be responsible for fixing C1.
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spelling pubmed-21396402008-04-17 THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M Hurst, Mary M. Volanakis, John E. Hester, Raymond B. Stroud, Robert M. Bennett, J. Claude J Exp Med Brief Definitive Reports An insight into the structural features of human IgM that are responsible for its capacity to bind the first component of complement (C) has been obtained by examining the ability of IgM subfragments to bind active C1 (C1). The smallest two fragments found to bind C1 were the major CNBr fragment of the Fc portion of IgM and the C(H)4 fragment of the carboxy-terminal domain. The smallest fragment which fixes C1 has a disaggregated mol wt of 6,800, consists of 60 residues, and contains no carbohydrate. Structural considerations and sequence overlaps suggest that the amino-terminal side of the C(H)4 domain (24 amino acid residues) might be responsible for fixing C1. The Rockefeller University Press 1974-10-01 /pmc/articles/PMC2139640/ /pubmed/4427090 Text en Copyright © 1974 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Brief Definitive Reports
Hurst, Mary M.
Volanakis, John E.
Hester, Raymond B.
Stroud, Robert M.
Bennett, J. Claude
THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M
title THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M
title_full THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M
title_fullStr THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M
title_full_unstemmed THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M
title_short THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M
title_sort structural basis for binding of complement by immunoglobulin m
topic Brief Definitive Reports
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139640/
https://www.ncbi.nlm.nih.gov/pubmed/4427090
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