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Interaction between separated consecutive complement control modules of human C1r: implications for dimerization of the full-length protease |
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| Authors: | Láng András Major Balázs Szilágyi Katalin Gáspári Zoltán Gál Péter Závodszky Péter Perczel András |
| Institution: | a Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány 1/A, H-1117 Budapest, Hungary b Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest H-1518, Hungary c Protein Modeling Group HAS-ELTE, Institute of Chemistry, Eötvös Loránd University, H-1538 Budapest, P.O. Box 32, Hungary |
| Abstract: | Complement control protein modules (CCP) typically mediate protein:protein interaction during immune response in vertebrates. Using NMR chemical shift perturbation mapping, we present previously lacking experimental evidence for intermolecular interactions between the CCP1 and CCP2 modules of the human C1r serine protease (SP). The identified interface is clearly distinct from that observed in the covalently linked CCP1-CCP2 pair. Structural models of the CCP1-CCP2-SP segments of two C1r molecules built on the basis of shift perturbation data are fully consistent with an extended interaction interface and suggests the possibility of a structural rearrangement as a switch between functional states of human C1r.Structured summaryMINT-8045767: CCP1 (uniprotkb:P00736) and CCP2 (uniprotkb:P00736) bind (MI:0407) by nuclear magnetic resonance (MI:0077) |
| Keywords: | CCP complement control protein module SP serine protease C1 first complex of the classical pathway of complement C1q recognition subunit of C1 C1r first catalytic subunit of C1 C1s second catalytic subunit of C1 EGF a module named after epidermal growth factor CUB a module of C1r/C1s urchin-type EGF bone morphogenic protein Ca2+ calcium ion α N-terminal autolytic fragment of C1r composed of CUB1 EGF and a short segment of CUB2 β autolytic fragment of C1r composed of most of the CUB2 γ autolytic fragment of C1r composed of CCP1 CCP2 and an intermediary segment also called activation peptide A chain N-terminal chain of active C1r composed of α β and γ fragments B chain the shorter C-terminal chain of active C1r which is the serine protease domain γB a disulfide linked fragment of γ and B PDB protein data bank HSQC heteronuclear single-quantum correlation (spectroscopy) MASP-2 2nd mannan-binding lectin associated serine protease |
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