ArticleNature chemical biology2016
A topological and conformational stability alphabet for multipass membrane proteins.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Design principles of the common Gly-X6-Gly membrane protein building block.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Discovery and Visualization of the Hidden Relationships among N-Glycosylation, Disulfide Bonds, and Membrane Topology.International journal of molecular sciences · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- All-Atom Molecular Dynamics Elucidating Molecular Mechanisms of Single-Transmembrane Model Peptide Dimerization in a Lipid Bilayer.ACS omega · 2021Article
- Small-residue packing motifs modulate the structure and function of a minimal de novo membrane protein.Scientific reports · 2020Article
- Designing minimalist membrane proteins.Biochemical Society transactions · 2019Review
- Tertiary Structural Motif Sequence Statistics Enable Facile Prediction and Design of Peptides that Bind Anti-apoptotic Bfl-1 and Mcl-1.Structure (London, England : 1993) · 2019Article
- Packing of apolar side chains enables accurate design of highly stable membrane proteins.Science (New York, N.Y.) · 2019Article
- Applications of sequence coevolution in membrane protein biochemistry.Biochimica et biophysica acta. Biomembranes · 2018Review
- Accurate computational design of multipass transmembrane proteins.Science (New York, N.Y.) · 2018Article
- Membrane-spanning α-helical barrels as tractable protein-design targets.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- G Protein-Coupled Receptors Contain Two Conserved Packing Clusters.Biophysical journal · 2017Article
- Protein structural motifs in prediction and design.Current opinion in structural biology · 2017Review
- Article
- Tertiary alphabet for the observable protein structural universe.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Toward high-resolution computational design of the structure and function of helical membrane proteins.Nature structural & molecular biology · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Multipass membrane proteins perform critical signal transduction and transport across membranes. How transmembrane helix (TMH) sequences encode the topology and conformational flexibility regulating these functions remains poorly understood. Here we describe a comprehensive analysis of the sequence-structure relationships at multiple interacting TMHs from all membrane proteins with structures in the Protein Data Bank (PDB). We found that membrane proteins can be deconstructed in interacting TMH trimer units, which mostly fold into six distinct structural classes of topologies and conformations. Each class is enriched in recurrent sequence motifs from functionally unrelated proteins, revealing unforeseen consensus and evolutionary conserved networks of stabilizing interhelical contacts. Interacting TMHs' topology and local protein conformational flexibility were remarkably well predicted in a blinded fashion from the identified binding-hotspot motifs. Our results reveal universal sequence-structure principles governing the complex anatomy and plasticity of multipass membrane proteins that may guide de novo structure prediction, design, and studies of folding and dynamics.
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