ArticleBiophysical journal2008
Lipid interaction networks of peripheral membrane proteins revealed by data-driven micelle docking.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Transmembrane Membrane Readers form a Novel Class of Proteins That Include Peripheral Phosphoinositide Recognition Domains and Viral Spikes.Membranes · 2022Review
- Article
- Integrative modeling of membrane-associated protein assemblies.Nature communications · 2020Article
- Phosphorylation of conserved phosphoinositide binding pocket regulates sorting nexin membrane targeting.Nature communications · 2018Article
- Structure of an Intrinsically Disordered Stress Protein Alone and Bound to a Membrane Surface.Biophysical journal · 2016Article
- Dynamics and Membrane Interactions of Protein Kinase C.Biochemistry · 2015Review
- Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.Nature communications · 2014Article
- Interfacial partitioning of a loop hinge residue contributes to diacylglycerol affinity of conserved region 1 domains.The Journal of biological chemistry · 2014Article
- A simple guide to biochemical approaches for analyzing protein-lipid interactions.Molecular biology of the cell · 2012Review
- Conditional peripheral membrane proteins: facing up to limited specificity.Structure (London, England : 1993) · 2012Review
- Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains.EMBO reports · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Many signaling and trafficking proteins contain modular domains that bind reversibly to cellular membranes. The structural basis of the intermolecular interactions which mediate these membrane-targeting events remains elusive since protein-membrane complexes are not directly accessible to standard structural biology techniques. Here we report a fast protein-micelle docking methodology that yields three-dimensional model structures of proteins inserted into micelles, revealing energetically favorable orientations, convergent insertion angles, and an array of protein-lipid interactions at atomic resolution. The method is applied to two peripheral membrane proteins, the early endosome antigen 1 (EEA1) FYVE (a zinc finger domain found in the proteins Fab1, YOTB/ZK632.12, Vac1, and EEA1) and Vam7p phagocyte oxidase homology domains, which are revealed to form extensive networks of interactions with multiple phospholipid headgroups and acyl chains. The resulting structural models explain extensive published mutagenesis data and reveal novel binding determinants. The docking restraints used here were based on NMR data, but can be derived from any technique that detects insertion of protein residues into a membrane, and can be applied to virtually any peripheral membrane protein or membrane-like structure.
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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 OpenQuestion graph.