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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Cooperative effects in the substrate specificity of the complement protease C1s

Sarah E. Boyd
  • Clayton School of Information Technology, Monash University, Clayton, Victoria 3800, Australia
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/ Felicity K. Kerr
  • Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia
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/ David W. Albrecht
  • Clayton School of Information Technology, Monash University, Clayton, Victoria 3800, Australia
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/ Maria Garcia de la Banda
  • Clayton School of Information Technology, Monash University, Clayton, Victoria 3800, Australia
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/ Natasha Ng
  • Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia
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/ Robert N. Pike
  • Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia
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Published Online: 2009-04-10 | DOI: https://doi.org/10.1515/BC.2009.064

Abstract

Complement is a key component of the immune system, but can contribute to inflammatory diseases. The substrate specificity of C1s protease has been successfully investigated using a combinatorial approach, while a positional scanning method failed. The lack of success of the latter approach is possibly due to cooperativity in the active site, which could confound such analyses. With a panel of peptides devised using factorial design, we show pronounced cooperativity between the S4 and S1′ subsites in the active site of the enzyme, and weaker cooperativity between the S1′ and S3′ subsites. The use of factorial design has promise as a methodology for determining cooperativity in protease active sites.

Keywords: active site; C1s; complement; cooperativity; protease; substrate specificity

About the article

Corresponding author


Received: 2008-11-25

Accepted: 2009-03-19

Published Online: 2009-04-10

Published in Print: 2009-01-01


Citation Information: Biological Chemistry, Volume 390, Issue 5/6, Pages 503–507, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.064.

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Biochemistry, 2011, Volume 50, Number 48, Page 10499

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