Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structural and functional studies of complement inhibitor C4b-binding protein.

A M Blom1

  • 1Department of Clinical Chemistry, Lund University, The Wallenberg Laboratory, University Hospital Malmö, Sweden. anna.blom@klkemi.mas.lu.se

Biochemical Society Transactions
|November 21, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

CD59 double knockout mice express a CD59ba hybrid fusion protein that mediates insulin secretion.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2024
Same author

Complement in metabolic disease: metaflammation and a two-edged sword.

Seminars in immunopathology·2021
Same author

The role of complement inhibitors beyond controlling inflammation.

Journal of internal medicine·2017
Same author

Cartilage oligomeric matrix protein contributes to the development and metastasis of breast cancer.

Oncogene·2016
Same author

Factor H uptake regulates intracellular C3 activation during apoptosis and decreases the inflammatory potential of nucleosomes.

Cell death and differentiation·2016
Same author

A novel method for direct measurement of complement convertases activity in human serum.

Clinical and experimental immunology·2014

C4b-binding protein (C4BP) inhibits the complement system. Researchers mapped C4BP

Area of Science:

  • Immunology and Biochemistry

Background:

  • C4b-binding protein (C4BP) is a key regulator of the classical complement pathway.
  • C4BP is a large glycoprotein composed of alpha and beta chains, featuring complement control protein (CCP) domains.

Purpose of the Study:

  • To identify and characterize the binding sites of C4BP for its ligands: complement factor C4b, heparin, and protein S.
  • To elucidate the functional consequences of these interactions on C4BP's inhibitory activity and pathogen interactions.

Main Methods:

  • Utilized homology-based computer modeling and mutagenesis of recombinant proteins.
  • Investigated ligand binding interactions through biochemical and functional assays.

Main Results:

  • C4b binding requires CCP1-3 of the alpha-chain, mediated by ionic interactions involving charged amino acids.

Related Experiment Videos

  • Heparin binding also involves CCP1-3 of the alpha-chain and the charged amino acid cluster.
  • Protein S binds with high affinity to CCP1 of the beta-chain via hydrophobic interactions.
  • Loss of C4b binding abrogates C4BP's classical pathway inhibitory function.
  • C4BP interacts with various bacterial pathogens (e.g., Neisseria gonorrhoeae, Streptococcus pyogenes) via its alpha-chain.

    • Conclusions:

    • The study precisely maps the molecular interactions of C4BP with key ligands.
    • These findings reveal the structural basis for C4BP's complement inhibitory functions and its role in pathogen evasion.