MHC Class III products: an electron microscopic study of the C3 convertases of human complement

We have reported a transmission electron microscopic study of the two C3 convertases of human complement and their precursors. The corresponding proteins and complexes of the classical and alternative pathway appear very similar. Cofactors C3b and C4b are nearly indistinguishable and display a chara...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1984
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187187/
https://www.ncbi.nlm.nih.gov/pubmed/6559206
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description We have reported a transmission electron microscopic study of the two C3 convertases of human complement and their precursors. The corresponding proteins and complexes of the classical and alternative pathway appear very similar. Cofactors C3b and C4b are nearly indistinguishable and display a characteristic but highly irregular substructure. C2 and Factor B are globular with diameters of 85 +/- 8 A and 80 +/- 8 A and both consist of three discrete globular domains each approximately 40 A in diameter. Bb and C2a each contain two domains connected by a short linker segment. Both domains of Bb and one domain of C2a are 42 A in diameter (28 kd), while the second domain of C2 is 47 A in diameter (39 kd). Attachment of the enzymatic subunits to cofactors occurs through one domain only.
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spelling pubmed-21871872008-04-17 MHC Class III products: an electron microscopic study of the C3 convertases of human complement J Exp Med Articles We have reported a transmission electron microscopic study of the two C3 convertases of human complement and their precursors. The corresponding proteins and complexes of the classical and alternative pathway appear very similar. Cofactors C3b and C4b are nearly indistinguishable and display a characteristic but highly irregular substructure. C2 and Factor B are globular with diameters of 85 +/- 8 A and 80 +/- 8 A and both consist of three discrete globular domains each approximately 40 A in diameter. Bb and C2a each contain two domains connected by a short linker segment. Both domains of Bb and one domain of C2a are 42 A in diameter (28 kd), while the second domain of C2 is 47 A in diameter (39 kd). Attachment of the enzymatic subunits to cofactors occurs through one domain only. The Rockefeller University Press 1984-01-01 /pmc/articles/PMC2187187/ /pubmed/6559206 Text en 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 Articles
MHC Class III products: an electron microscopic study of the C3 convertases of human complement
title MHC Class III products: an electron microscopic study of the C3 convertases of human complement
title_full MHC Class III products: an electron microscopic study of the C3 convertases of human complement
title_fullStr MHC Class III products: an electron microscopic study of the C3 convertases of human complement
title_full_unstemmed MHC Class III products: an electron microscopic study of the C3 convertases of human complement
title_short MHC Class III products: an electron microscopic study of the C3 convertases of human complement
title_sort mhc class iii products: an electron microscopic study of the c3 convertases of human complement
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187187/
https://www.ncbi.nlm.nih.gov/pubmed/6559206

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