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

Arg343 in human surfactant protein D governs discrimination between glucose and N-acetylglucosamine ligands.

Glycobiology - 1 Aug 2004

Allen Martin J, Laederach Alain, Reilly Peter J, Mason Robert J, Voelker Dennis R

Abstract excerpt

Surfactant protein D (SP-D), one of the members of the collectin family of C-type lectins, is an important component of pulmonary innate immunity. SP-D binds carbohydrates in a calcium-dependent manner, but the mechanisms governing its ligand recognition specificity are not well understood. SP-D binds glucose (Glc) stronger than N-acetylglucosamine (GlcNAc). Structural superimposition of hSP-D with mannose-...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosamine
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Arginine

Share to Computer Simulation

Share to Glucose

Share to Ligands

Share to Mutagenesis, Site-Directed

Share to Pulmonary Surfactant-Associated Protein D

Source

Identifiers

PMID: 15115749
DOI: 10.1093/glycob/cwh088

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Arg343 in human surfactant protein D governs discrimination between glucose and N-acetylglucosamine ligands.PMID 15115749Read ↗

Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: contributions of an extended site and residue 343.Semantic proximity Read ↗

Ligand specificity of human surfactant protein D: expression of a mutant trimeric collectin that shows enhanced interactions with influenza A virus.Semantic proximity Read ↗

Differential Ligand Binding Specificities of the Pulmonary Collectins Are Determined by the Conformational Freedom of a Surface Loop.Semantic proximity Read ↗

Surfactant protein-D and pulmonary host defense.Semantic proximity Read ↗

Recombinant SP-D carbohydrate recognition domain is a chemoattractant for human neutrophils.Semantic proximity Read ↗

Monoclonal antibody-assisted structure-function analysis of the carbohydrate recognition domain of surfactant protein D.Semantic proximity Read ↗

Elucidation of Lipid Binding Sites on Lung Surfactant Protein A Using X-ray Crystallography, Mutagenesis, and Molecular Dynamics Simulations.Semantic proximity Read ↗

Multimeric and trimeric subunit SP-D are interconvertible structures with distinct ligand interaction.Semantic proximity Read ↗

Human pulmonary surfactant protein D binds the extracellular domains of Toll-like receptors 2 and 4 through the carbohydrate recognition domain by a mechanism different from its binding to phosphatidylinositol and lipopolysaccharide.Semantic proximity Read ↗

Structure, genetics and function of the pulmonary associated surfactant proteins A and D: The extra-pulmonary role of these C type lectins.Semantic proximity Read ↗

Introduction of N-linked glycans in the lectin domain of surfactant protein D: impact on interactions with influenza A viruses.Semantic proximity Read ↗

Complementation of Pulmonary Abnormalities in SP-D(−/−) Mice with an SP-D/Conglutinin Fusion ProteinSemantic proximity Read ↗

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