PMID: 9445402Mar 7, 1998Paper

Native conformations of human complement components C3 and C4 show different dependencies on thioester formation

The Biochemical Journal
L IsaacD E Isenman

Abstract

The thioester bond in complement components C3 and C4 and the protease inhibitor alpha2-macroglobulin have traditionally been thought of as fulfilling the dual roles of mediating covalent attachment and maintaining the native conformational states of these molecules. We previously reported that several human C3 thioester-region mutants, including variants E1012Q and C1010A, in the latter of which thioester-bond formation is precluded, display an unexpected phenotype. Despite the lack of a thioester bond in these mutants, they appear to adopt a native-like conformation as suggested by the finding that they are cleavable by the classical pathway C3 convertase, C4b2a, whereas the C3b-like C3(H2O) species is not. Subsequently, a species referred to as C3(NH3)* was described which potentially could account for the observations with the above mutants. C3(NH3)* is a transient species formed on aminolysis of native C3 that can spontaneously re-form the thioester bond. Importantly, it has a mobility on cation-exchange HPLC that is distinct from both native C3 and C3(H2O), but like the native molecule, it is cleavable by an alternative-pathway C3 convertase. In this study we showed by using cation-exchange HPLC as an additional conformat...Continue Reading

Citations

Jul 13, 2006·Journal of Molecular Biology·Folmer FredslundLars Sottrup-Jensen
Jun 3, 2016·Molecular & Cellular Proteomics : MCP·Zhuo A ChenJuri Rappsilber
Dec 14, 2004·Chembiochem : a European Journal of Chemical Biology·Peter SawatzkiThomas Kolter
Jun 10, 2008·Nature Immunology·Folmer FredslundGregers R Andersen
Apr 26, 2019·Frontiers in Immunology·Michelle ElvingtonJohn P Atkinson

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