Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.

doi:10.1074/jbc.M607686200

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

Back to search

Article

Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.

The Journal of biological chemistry - 1 Dec 2006

Hagemann Ian S, Narzinski Kirk D, Floyd Desiree H, Baranski Thomas J

Abstract excerpt

The N terminus of G protein-coupled receptors has been implicated in binding to peptide hormones. We have used random saturation mutagenesis to identify essential residues in the N terminus of the human complement factor 5a receptor (C5aR). In a library of N-terminal mutant C5aR molecules screened for activation by C5a, residues 24-30 of the C5aR showed a marked propensity to mutate to cysteine, most likely...

Topics

Amino Acid Sequence
Bacterial Proteins
Complement C5a
Cysteine
Disulfides
Gene Library
Humans
Ligands
Luminescent Proteins
Membrane Proteins
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis

Mutation

Protein Binding

Protein Conformation

Protein Structure, Tertiary

Receptor, Anaphylatoxin C5a

Source

Open in PubMed

Identifiers

PMID: 17023413
DOI: 10.1074/jbc.M607686200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.PMID 17023413Read ↗

The amino terminus of the human C5a receptor is required for high affinity C5a binding and for receptor activation by C5a but not C5a analogs.Semantic proximity Read ↗

Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function.Semantic proximity Read ↗

C5a receptor activation. Genetic identification of critical residues in four transmembrane helices.Semantic proximity Read ↗

Genetic analysis of the first and third extracellular loops of the C5a receptor reveals an essential WXFG motif in the first loop.Semantic proximity Read ↗

High throughput mutational characterization of the GPCR ligand C5a using yeast display and deep sequencing.Semantic proximity Read ↗

Third extracellular loop (EC3)-N terminus interaction is important for seven-transmembrane domain receptor function: implications for an activation microswitch region.Semantic proximity Read ↗

Arginine 206 of the C5a receptor is critical for ligand recognition and receptor activation by C-terminal hexapeptide analogs.Semantic proximity Read ↗

Structural insights into agonist-binding and activation of the human complement C3a receptorSemantic proximity Read ↗

Molecular mechanism of naturally-encoded signaling-bias at the complement anaphylatoxin receptorsSemantic proximity Read ↗

Essential role for the second extracellular loop in C5a receptor activation.Semantic proximity Read ↗

Partial ligand-receptor engagement yields functional bias at the human complement receptor, C5aR1Semantic proximity Read ↗

Structure of the complement C5a receptor bound to the extra-helical antagonist NDT9513727.Semantic proximity Read ↗

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