Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Positively charged amino acids at the interface between alpha-chain CCP1 and CCP2 of C4BP are required for regulation of the classical C3-convertase.

Molecular immunology - 1 Jun 2000

Blom A M, Zadura A F, Villoutreix B O, Dahlbäck B

Abstract excerpt

C4b-binding protein (C4BP) is an abundant and potent down-regulator of complement activation. In its presence, the assembly of the classical pathway C3-convertase is prevented and its natural decay is accelerated. C4BP also acts as a cofactor to the serine proteinase factor I in the cleavage of C...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Binding Sites
Share to Erythrocytes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fibrinogen

Share to Histocompatibility Antigens

Share to Protein Structure, Quaternary

Share to Static Electricity

Source

Identifiers

PMID: 11090879
DOI: 10.1016/s0161-5890(00)00059-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Prepared record publication-11090879-2026-09-05.1. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Positively charged amino acids at the interface between alpha-chain CCP1 and CCP2 of C4BP are required for regulation of the classical C3-convertase.PMID 11090879Read ↗

A cluster of positively charged amino acids in the alpha-chain of C4b-binding protein (C4BP) is pivotal for the regulation of the complement system and the interaction with bacteria.Semantic proximity Read ↗

CCP1-4 of the C4b-binding protein alpha-chain are required for factor I mediated cleavage of complement factor C3b.Semantic proximity Read ↗

Mutations in alpha-chain of C4BP that selectively affect its factor I cofactor function.Semantic proximity Read ↗

Structural and functional studies of complement inhibitor C4b-binding proteinSemantic proximity Read ↗

Structural Requirements for the Complement Regulatory Activities of C4BPSemantic proximity Read ↗

Human C4b-Binding Protein Has Overlapping, But Not Identical, Binding Sites for C4b and Streptococcal M ProteinsSemantic proximity Read ↗

C4b-binding protein: The good, the bad and the deadly. Novel functions of an old friend.Semantic proximity Read ↗

Structural Basis for the Function of Complement Component C4 within the Classical and Lectin Pathways of ComplementSemantic proximity Read ↗

The amino-terminal module of the C4b-binding protein α-chain is crucial for C4b binding and factor I-cofactor functionSemantic proximity Read ↗

New functional and structural insights from updated mutational databases for complement factor H, Factor I, membrane cofactor protein and C3Semantic proximity Read ↗

Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sitesSemantic proximity Read ↗

Structure-Function Analysis of the Active Sites of Complement Receptor Type 1Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.