
Design protein binders targeting RBX1, a cancer-relevant E3 ubiquitin ligase component. Co-organized with the GEM Workshop at ICLR 2026.
Submit your protein binder designs targeting RBX1. Each team submits a method description (PDF, 2 pages max) and a ranked binder list (CSV, ≤100 sequences, ≤250 AA each). Designs must be de novo with a minimum edit distance of 25% to UniRef50 (25% CDR edit distance to SAbDab for single-domain antibodies).
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A total of 300 designs are tested experimentally via bio-layer interferometry at Adaptyv's Foundry. Results announced at ICLR 2026 in Rio de Janeiro.
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Submit your protein binder designs targeting RBX1. Each team submits a method description (PDF, 2 pages max) and a ranked binder list (CSV, ≤100 sequences, ≤250 AA each). Designs must be de novo with a minimum edit distance of 25% to UniRef50 (25% CDR edit distance to SAbDab for single-domain antibodies).
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A total of 300 designs are tested experimentally via bio-layer interferometry at Adaptyv's Foundry. Results announced at ICLR 2026 in Rio de Janeiro.
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PDB: 2LGV
RBX1 (RING Box Protein 1) is a 108-amino acid component of the Cullin-RING E3 ubiquitin ligase (CRL) complex, the largest family of E3 ligases in humans. CRLs control degradation of roughly 20% of all cellular proteins, regulating cell cycle progression, DNA repair, and signal transduction. RBX1 recruits E2 ubiquitin-conjugating enzymes to the complex, serving as its catalytic subunit.
In this competition, co-organized with the GEM Workshop at ICLR 2026, the goal is to design protein binders against RBX1. The protein combines an intrinsically disordered N-terminal region with a stabilized C-terminal RING-H2 finger domain coordinating three zinc ions, a dual structural challenge for binder design. Disrupting RBX1 function could inhibit CRL-mediated protein degradation, with applications in cancer therapy where CRL activity is frequently dysregulated.
Teams submit up to 100 ranked binder sequences (≤250 AA each). Designs must be de novo — motif scaffolding and lead optimization are not allowed, with the exception of single-domain antibodies. Binder sequences must have a minimum edit distance of 25% of total sequence length to known proteins in UniRef50; for single-domain antibodies, CDR loops must have a minimum edit distance of 25% to known antibodies in SAbDab. Selected designs undergo experimental validation via bio-layer interferometry at Adaptyv's Foundry. Results will be announced at ICLR 2026 in Rio de Janeiro on April 26. All submitted sequences and experimental data are published as open-source on Proteinbase under the ODC-ODbL license.
Rules
Submit your protein binder designs targeting RBX1. Each team submits a method description (PDF, 2 pages max) and a ranked binder list (CSV, ≤100 sequences, ≤250 AA each). Designs must be de novo with a minimum edit distance of 25% to UniRef50 (25% CDR edit distance to SAbDab for single-domain antibodies).
Submissions selected by a panel of experts for their novelty and originality