Identification of receptor-binding residues in the inflammatory complement protein C5a by site-directed mutagenesis
about
Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminusIdentification of receptor-binding sites of monocyte chemotactic S19 ribosomal protein dimerStructural and functional characterization of human and murine C5a anaphylatoxinsStructural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopyC5a mutants are potent antagonists of the C5a receptor (CD88) and of C5L2: position 69 is the locus that determines agonism or antagonismResidues 21-30 within the extracellular N-terminal region of the C5a receptor represent a binding domain for the C5a anaphylatoxinInterleukin 1 receptor antagonist is a member of the interleukin 1 gene family: evolution of a cytokine control mechanismAn activation switch in the ligand binding pocket of the C5a receptor.Cloning and functional expression of the canine anaphylatoxin C5a receptor. Evidence for high interspecies variability.Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.Structure of the complement factor 5a receptor-ligand complex studied by disulfide trapping and molecular modeling.Restricted ability of group B streptococcal C5a-ase to inactivate C5a prepared from different animal species.Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens.Two-site binding of C5a by its receptor: an alternative binding paradigm for G protein-coupled receptors.Pharmacological characterization of antagonists of the C5a receptorSite-specific mutations in the N-terminal region of human C5a that affect interactions of C5a with the neutrophil C5a receptor.Sulfated tyrosines contribute to the formation of the C5a docking site of the human C5a anaphylatoxin receptor.The role of complement, C5a and its receptors in sepsis and multiorgan dysfunction syndrome.Cell-free synthesis of isotopically labelled peptide ligands for the functional characterization of G protein-coupled receptors.Enhancement of in vivo and in vitro immune functions by a conformationally biased, response-selective agonist of human C5a: implications for a novel adjuvant in vaccine design.Structural basis for the targeting of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer.Structural mechanisms of constitutive activation in the C5a receptors with mutations in the extracellular loops: molecular modeling study.Comparative agonist/antagonist responses in mutant human C5a receptors define the ligand binding site.Allosterism in human complement component 5a ((h)C5a): a damper of C5a receptor (C5aR) signaling.Identification of ligand effector binding sites in transmembrane regions of the human G protein-coupled C3a receptor.Probing the "message:address" sites for chemoattractant binding to the C5a receptor. Mutagenesis of hydrophilic and proline residues within the transmembrane segments.Mutation of glutamate 199 of the human C5a receptor defines a binding site for ligand distinct from the receptor N terminus.Complement C5a receptor assay for high throughput screening.Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding.Structural models for the complex of chemotaxis inhibitory protein of Staphylococcus aureus with the C5a receptor.A recombinant hybrid anaphylatoxin with dual C3a/C5a activity.The pharmacophore of the human C5a anaphylatoxin.Pivotal Advance: Interconversion between pure chemotactic ligands and chemoattractant/secretagogue ligands of neutrophil C5a receptor by a single amino acid substitution.Site-specific disulfide capture of agonist and antagonist peptides on the C5a receptor.Identification of novel inhibitors of the translationally controlled tumor protein (TCTP): insights from molecular dynamics.The Model Structures of the Complement Component 5a Receptor (C5aR) Bound to the Native and Engineered hC5a.Structure and characterization of a high affinity C5a monoclonal antibody that blocks binding to C5aR1 and C5aR2 receptors.The influence of Lys68 in decepeptide agonists of C5a on C5a receptor binding, activation and selectivity.
P2860
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P2860
Identification of receptor-binding residues in the inflammatory complement protein C5a by site-directed mutagenesis
description
1989 nî lūn-bûn
@nan
1989 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Identification of receptor-bin ...... a by site-directed mutagenesis
@ast
Identification of receptor-bin ...... a by site-directed mutagenesis
@en
type
label
Identification of receptor-bin ...... a by site-directed mutagenesis
@ast
Identification of receptor-bin ...... a by site-directed mutagenesis
@en
prefLabel
Identification of receptor-bin ...... a by site-directed mutagenesis
@ast
Identification of receptor-bin ...... a by site-directed mutagenesis
@en
P2093
P2860
P356
P1476
Identification of receptor-bin ...... a by site-directed mutagenesis
@en
P2093
Mandecki W
Mollison KW
Shallcross MA
Zuiderweg ER
P2860
P304
P356
10.1073/PNAS.86.1.292
P407
P577
1989-01-01T00:00:00Z