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Updated: Jan 20, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Structural Analysis of Tilvestamab in Complex with AXL.

Eleni Christakou1,2, Andrea J Lopez1, Gopinath Muruganandam3,4

  • 1Department of Biomedicine, University of Bergen, Bergen 5020, Norway.

ACS Omega
|January 19, 2026
PubMed
Summary
This summary is machine-generated.

This study characterizes the AXL-tilvestamab complex, a potential cancer therapy. Structural analysis using cryo-EM and SAXS provides a low-resolution model, guiding future drug development for AXL signaling.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Oncology

Background:

  • AXL receptor tyrosine kinase (RTK) plays a key role in cancer cell signaling.
  • Growth arrest-specific protein 6 (GAS6) is the ligand for AXL.
  • Tilvestamab (BGB149) is a novel therapeutic antibody targeting AXL.

Purpose of the Study:

  • To structurally characterize the complex formed between AXL and the anti-AXL antibody, tilvestamab.
  • To provide a foundation for optimizing high-resolution structural studies and drug design.

Main Methods:

  • Negative-stain and cryogenic transmission electron microscopy (cryo-EM).
  • Synchrotron small-angle X-ray scattering (SAXS).
  • Utilized monomeric soluble AXL extracellular domain, tilvestamab Fab fragment, and anti-Fab nanobody for homogeneous sample preparation.

Main Results:

  • Confirmed successful complex formation between AXL and tilvestamab using SAXS and cryo-EM.
  • Generated a low-resolution 3D model of the tilvestamab-AXL complex.
  • Identified methods for creating homogeneous samples suitable for structural biology.

Conclusions:

  • Structural insights into the AXL-tilvestamab complex were obtained.
  • The study facilitates optimization for high-resolution structural determination.
  • Findings support the rational design of mutations to modulate antibody binding affinity and specificity for AXL.