Effect of reactive site loop elongation on the inhibitory activity of C1-inhibitor

Bos, Ineke G. A. and Lubbers, Yvonne T. P. and Eldering, Eric and Abrahams, Jan Pieter and Hack, C. Erik. (2004) Effect of reactive site loop elongation on the inhibitory activity of C1-inhibitor. Biochimica et Biophysica Acta - Proteins and Proteomics, 1699 (1-2). pp. 139-144.

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The serine protease inhibitor C1-Inhibitor (C1-Inh) inhibits several complement- and contact-system proteases, which play an important role in inflammation. C1-Inh has a short reactive site loop (RSL) compared to other serpins. RSL length determines the inhibitory activity of serpins. We investigated the effect of RSL elongation on inhibitory activity of C1-Inh by insertion of one or two alanine residues in the RSL. One of five mutants had an increased association rate with kallikrein, but was nevertheless a poor inhibitor because of a simultaneous high stoichiometry of inhibition (>10). The association rate of the other variants was lower than that of wild-type C1-Inh. These data suggest that the relatively weak inhibitory activity of C1-Inh is not the result of its short RSL. The short RSL of C1-Inh has, surprisingly, the optimal length for inhibition. (C) 2004 Elsevier B.V. All rights reserved.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:05 Nov 2020 15:59
Deposited On:05 Nov 2020 15:59

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