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

András Láng, Balázs Major, Katalin Szilágyi, Z. Gáspári, P. Gál, P. Závodszky, A. Perczel

Research output: Contribution to journalArticle

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

Fingerprint

Dimerization
Serine Proteases
Peptide Hydrolases
Structural Models
Nuclear magnetic resonance
Vertebrates
Complement System Proteins
Proteins
Magnetic Resonance Spectroscopy
Chemical shift
Switches
Molecules

Keywords

  • Complement
  • Docking
  • NMR perturbation
  • Protein:protein interaction

ASJC Scopus subject areas

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

Cite this

Interaction between separated consecutive complement control modules of human C1r : Implications for dimerization of the full-length protease. / Láng, András; Major, Balázs; Szilágyi, Katalin; Gáspári, Z.; Gál, P.; Závodszky, P.; Perczel, A.

In: FEBS Letters, Vol. 584, No. 22, 19.11.2010, p. 4565-4569.

Research output: Contribution to journalArticle

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AU - Láng, András

AU - Major, Balázs

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AU - Gáspári, Z.

AU - Gál, P.

AU - Závodszky, P.

AU - Perczel, A.

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AB - 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).

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