The Structure of Bovine Complement Component 3 Reveals the Basis for Thioester Function
- 1 August 2006
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 361 (1), 115-127
- https://doi.org/10.1016/j.jmb.2006.06.009
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Functional Insights from the Structure of the Multifunctional C345C Domain of C5 of ComplementPublished by Elsevier BV ,2005
- Therapeutic potential of targeting the complement cascade in critical care medicineCritical Care Medicine, 2003
- X-ray Crystal Structure of the C4d Fragment of Human Complement Component C4Journal of Molecular Biology, 2002
- Cell surface antigen CD109 is a novel member of the α2 macroglobulin/C3, C4, C5 family of thioester-containing proteinsBlood, 2002
- Crystal structure of the receptor-binding domain of α2-macroglobulinStructure, 1998
- The reaction mechanism of the internal thioester in the human complement component C4Nature, 1996
- Covalent binding properties of the human complement protein C4 and hydrolysis rate of the internal thioester upon activationProtein Science, 1993
- Peptide models of protein metastable binding sites: competitive kinetics of isomerization and hydrolysisBiochemistry, 1986
- Trypsin‐induced activation of the thiol esters in α2‐macroglobulin generates a short‐lived intermediate (‘nascent’ α2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activityFEBS Letters, 1981
- A thiol‐ester in α2‐macroglobulin cleaved during proteinase complex formationFEBS Letters, 1980