ArticleNature chemistry2017
Computational design of self-assembling cyclic protein homo-oligomers.
Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed.
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- Site-specific labelling of native peptides and proteins: chemical and enzymatic strategies.Beilstein journal of organic chemistry · 2026Review
- De novo design of light-responsive protein-protein interactions enables reversible formation of protein assemblies.Nature chemistry · 2025Article
- Structural determination of small proteins by cryo-EM using a coiled coil module strategy.Scientific reports · 2025Article
- Bond-centric modular design of protein assemblies.Nature materials · 2025Article
- Nonfouling Coatings from Synthetic Intrinsically Disordered Proteins.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Oligomerization Function of the Native Exon 5 Sequence of Ameloblastin Fused with Calmodulin.ACS omega · 2025Article
- Apoprotein Intermolecular Interactions and Heme Insertion for 3D Domain Swapping in Myoglobin.ACS omega · 2025Article
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- Computational design of non-porous pH-responsive antibody nanoparticles.Nature structural & molecular biology · 2024Article
- De novo design of buttressed loops for sculpting protein functions.Nature chemical biology · 2024Article
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- De novo design of proteins housing excitonically coupled chlorophyll special pairs.Nature chemical biology · 2024Article
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- Molecular basis for curvature formation in SepF polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- De novo design of modular protein hydrogels with programmable intra- and extracellular viscoelasticity.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Precisely patterned nanofibres made from extendable protein multiplexes.Nature chemistry · 2023Article
25 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Self-assembling cyclic protein homo-oligomers play important roles in biology, and the ability to generate custom homo-oligomeric structures could enable new approaches to probe biological function. Here we report a general approach to design cyclic homo-oligomers that employs a new residue-pair-transform method to assess the designability of a protein-protein interface. This method is sufficiently rapid to enable the systematic enumeration of cyclically docked arrangements of a monomer followed by sequence design of the newly formed interfaces. We use this method to design interfaces onto idealized repeat proteins that direct their assembly into complexes that possess cyclic symmetry. Of 96 designs that were characterized experimentally, 21 were found to form stable monodisperse homo-oligomers in solution, and 15 (four homodimers, six homotrimers, six homotetramers and one homopentamer) had solution small-angle X-ray scattering data consistent with the design models. X-ray crystal structures were obtained for five of the designs and each is very close to their corresponding computational model.
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Registered trials
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 Socratic graph.