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Related Experiment Video

Updated: Apr 9, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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A structural code for assembly specificity in GID/CTLH-type E3 ligases.

Pia Maria van Gen Hassend1, Hermann Schindelin1

  • 1Institute of Structural Biology, Rudolf Virchow Center for Integrative and Translational Bioimaging, Julius-Maximilians-Universität Würzburg, Würzburg, Germany.

Elife
|April 8, 2026
PubMed
Summary
This summary is machine-generated.

Scientists decoded the assembly specificity code for GID/CTLH-type E3 ligases, revealing how conserved features dictate subunit arrangement in these ring-shaped protein complexes.

Keywords:
CTLH-CRA domainGID/CTLH complexMaeaRanBP9/10Twa1homo sapiensmolecular biophysicsmousemuskelinprotein engineeringratstructural biologyubiquitin E3 ligase

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In Vitro Analysis of E3 Ubiquitin Ligase Function
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • GID/CTLH-type E3 ligases form conserved ring-shaped structures from repeating modules.
  • The molecular rules governing specific subunit arrangement within these ligases were previously unknown.

Purpose of the Study:

  • To decode the structural 'assembly specificity code' responsible for CRA-CRA pairing in GID/CTLH-type E3 ligases.
  • To understand the molecular basis of high-affinity interactions and subunit selectivity.

Main Methods:

  • Crystal structures of multiple CTLH-CRA domains were determined.
  • Quantitative binding analyses were performed.
  • Targeted perturbations of conserved sequence and geometric features were utilized.

Main Results:

  • Several interfaces exhibit exceptionally high affinity, reaching the picomolar range.
  • Conserved sequence and geometric features ensure specific pairing between cognate subunits.
  • Perturbing these features reprogrammed pairing preferences, allowing non-native interactions.

Conclusions:

  • The study reveals the molecular logic preserving the architecture of GID/CTLH-type E3 ligases.
  • The assembly code is decipherable and engineerable, offering a foundation for reconfiguring these E3 ligases.