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

Basis of the Intrinsic Flexibility of the Cε3 Domain of IgE

26 Apr 2011

Abstract excerpt

Allergic reactions are triggered by the interaction between IgE and its high-affinity receptor, FcεRI. Various studies have mapped the interaction surface between IgE and its cellular receptors to the third constant domain of IgE (Cε3). The isolated Cε3 domain has been shown to exist as a molten globule, and the domain retains significant flexibility within the context of the IgE protein. Here we have analyzed...

Read the complete abstract on PubMed

Topics

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

Share to Asthma and respiratory diseases
Share to Mast cells and histamine
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21520934
DOI: 10.1021/bi200019y

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Basis of the Intrinsic Flexibility of the Cε3 Domain of IgEPMID 21520934Read ↗

Structural insights into the high-affinity IgE receptor FcεRI complex.Semantic proximity Read ↗

Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.Semantic proximity Read ↗

Identification of amino acid residues involved in the interaction of canine IgE with canine and human FcεRIα.Semantic proximity Read ↗

The human IgM pentamer is a mushroom-shaped molecule with a flexural bias.Semantic proximity Read ↗

Structural and Physical Basis for Anti-IgE Therapy.Semantic proximity Read ↗

The p.Arg435His Variation of IgG3 With High Affinity to FcRn Is Associated With Susceptibility for Pemphigus Vulgaris-Analysis of Four Different Ethnic Cohorts.Semantic proximity Read ↗

Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3).Semantic proximity Read ↗

The increased hinge flexibility of an IgG1-IgG3 hybrid monoclonal enhances Fc-mediated protection against group A streptococciSemantic proximity Read ↗

IgG2 Fc structure and the dynamic features of the IgG CH2-CH3 interface.Semantic proximity Read ↗

Structure of the C3b Binding Site of CR1 (CD35), the Immune Adherence ReceptorSemantic proximity Read ↗

Immunoglobulin E-binding site in Fc epsilon receptor (Fc epsilon RII/CD23) identified by homolog-scanning mutagenesis.Semantic proximity Read ↗

An improved Protein G with higher affinity for human/rabbit IgG Fc domains exploiting a computationally designed polar network.Semantic proximity Read ↗

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