Evidence map›Paper›PMID 29731233›Full record

ArticleStructure (London, England : 1993)2018

Conformational Plasticity of the Immunoglobulin Fc Domain in Solution.

Soumya G Remesh, Anthony A Armstrong, Andrew D Mahan, Jinquan Luo, Michal Hammel

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. C4BP occludes the non-opsonic interaction ofInfection and immunity · 2026
    Article
  2. C4BP occludes the non-opsonic interaction ofbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  5. Article
  6. Effects ofFrontiers in molecular biosciences · 2024
    Article
  7. Effects of glycans and hinge on dynamics in the IgG1 Fc.Journal of biomolecular structure & dynamics · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Contorsbody, an antibody format for agonism: Design, structure, and function.Computational and structural biotechnology journal · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. CmAbs · 2019
    Article
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Soumya G RemeshMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Anthony A ArmstrongJanssen BioTherapeutics, Janssen R&D, LLC, Spring House, PA 19477, USA.
Andrew D MahanJanssen BioTherapeutics, Janssen R&D, LLC, Spring House, PA 19477, USA.
Jinquan LuoJanssen BioTherapeutics, Janssen R&D, LLC, Spring House, PA 19477, USA. Electronic address: jluo@its.jnj.com.
Michal HammelMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: mhammel@lbl.gov.

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI WALTER J. CHAZIN · 2001 to 2026
$89.6M
User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
NCI NIH HHS P01 CA092584NIGMS NIH HHS P30 GM124169
6 · The paper itself

Abstract

Fragment crystallizable (Fc) region of immunoglobulin G (IgG) antibody binds to specific Fc receptors (FcγRs) to control antibody effector functions. Currently, engineered specific Fc-FcγR interactions are validated with a static conformation derived from the crystal structure. However, computational evidence suggests that the conformational variability of Fcs plays an important role in receptor recognition. Here we elucidate Fc flexibility of IgG1, IgG2, and IgG1 Fc with mutations (M255Y/S257T/T259E) in solution by small-angle X-ray scattering (SAXS). Measured SAXS profiles and experimental parameters show variations in flexibility between Fc isotypes. We develop and apply a modeling tool for an accurate conformational sampling of Fcs followed by SAXS fitting. Revealed conformational variability of the CH2 domain as low as 10 Å in displacement, illustrates the power of the atomistic modeling combined with SAXS. This inexpensive SAXS-based approach offers to improve the engineering of antibodies for tailoring Fc receptor interactions through altering and measuring Fc flexibility.

Indexed as

Crystallography, X-RayImmunoglobulin Fc FragmentsImmunoglobulin GModels, MolecularProtein BindingProtein ConformationScattering, Small AngleSolubilityX-Ray DiffractionImmunoglobulin Fc FragmentsImmunoglobulin GBILBOMDconformational flexibilityfragment crystallizable (Fc) regionglycoproteinimmunoglobulin G antibody (IgG)rigid body modelingSAXSsmall angle X-ray scattering

Identifiers

PMID29731233
PMCPMC7039147

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.