Interaction between separated consecutive complement control modules of human C1r: Implications for dimerization of the full-length protease

András Láng, Balázs Major, Katalin Szilágyi, Zoltán Gáspári, Péter Gál, Péter Závodszky, András Perczel

Research output: Article

3 Citations (Scopus)

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 summary: MINT- 8045767: CCP1 (uniprotkb: P00736) and CCP2 (uniprotkb: P00736) bind (MI: 0407) by nuclear magnetic resonance (MI: 0077).

Original languageEnglish
Pages (from-to)4565-4569
Number of pages5
JournalFEBS letters
Volume584
Issue number22
DOIs
Publication statusPublished - nov. 19 2010

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Interaction between separated consecutive complement control modules of human C1r: Implications for dimerization of the full-length protease'. Together they form a unique fingerprint.

  • Cite this