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

Multiple domains of MASP-2, an initiating complement protease, are required for interaction with its substrate C4.

Molecular immunology - 1 Jan 2012

Duncan Renee C, Bergström Frida, Coetzer Theresa H, Blom Anna M, Wijeyewickrema Lakshmi C, Pike Robert N

Abstract excerpt

The complement system is fundamental to both innate and adaptive immunity and can be initiated via the classical, lectin or alternative pathways. Cleavage of C4 by MASP-2, the initiating protease of the lectin pathway, is a crucial event in the activation of this pathway, preceding the eventual formation of the C3 convertase (C4bC2a) complex on the pathogen surface. Interactions required for the cleavage of C4 by...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Complement C4

Share to Lectins

Share to Mannose-Binding Protein-Associated Serine Proteases

Share to Protein Structure, Tertiary

Share to Recombinant Proteins

Share to Static Electricity

Source

Identifiers

PMID: 22071314
DOI: 10.1016/j.molimm.2011.10.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multiple domains of MASP-2, an initiating complement protease, are required for interaction with its substrate C4.PMID 22071314Read ↗

Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4.Semantic proximity Read ↗

Structural basis for activation of the complement system by component C4 cleavage.Semantic proximity Read ↗

A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations.Semantic proximity Read ↗

Mannan-Binding Lectin-Associated Serine Protease (MASP)-1 Is Crucial for Lectin Pathway Activation in Human Serum, whereas neither MASP-1 nor MASP-3 Is Required for Alternative Pathway FunctionSemantic proximity Read ↗

MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad SpecificitySemantic proximity Read ↗

Interaction of mannose-binding protein with associated serine proteases: effects of naturally occurring mutations.Semantic proximity Read ↗

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

Functional domains, structural variations and pathogen interactions of MCP, DAF and CR1.Semantic proximity Read ↗

Complement activation by ligand-driven juxtaposition of discrete pattern recognition complexesSemantic proximity Read ↗

Deciphering Complement Receptor Type 1 Interactions with Recognition Proteins of the Lectin Complement PathwaySemantic proximity Read ↗

Complement C7 and clusterin form a complex in circulationSemantic proximity Read ↗

Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway.Semantic proximity Read ↗

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