ArticleBiophysical journal2006
Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
58 citing papers in PubMed, 117 citations in OpenAlex.
- Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach.iScience · 2026Article
- Tetraspanins: structure, dynamics, and principles of partner-protein recognition.Trends in cell biology · 2024Review
- Membrane organization by tetraspanins and galectins shapes lymphocyte function.Nature reviews. Immunology · 2024Review
- Review
- Targeting of Tetraspanin CD81 with Monoclonal Antibodies and Small Molecules to Combat Cancers and Viral Diseases.Cancers · 2023Review
- A conserved sequence in the small intracellular loop of tetraspanins forms an M-shaped inter-helix turn.Scientific reports · 2022Article
- Construction of Yeast Display Libraries for Selection of Antigen-Binding Variants of Large Extracellular Loop of CD81, a Major Surface Marker Protein of Extracellular Vesicles.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Arabidopsis Tetraspanins Facilitate Virus InfectionFrontiers in plant science · 2022Article
- An engineered CD81-based combinatorial library for selecting recombinant binders to cell surface proteins: Laminin binding CD81 enhances cellular uptake of extracellular vesicles.Journal of extracellular vesicles · 2021Article
- CellectSeq: In silico discovery of antibodies targeting integral membrane proteins combining in situ selections and next-generation sequencing.Communications biology · 2021Article
- Tetraspanins as Potential Modulators of Glutamatergic Synaptic Function.Frontiers in molecular neuroscience · 2021Review
- Open conformation of tetraspanins shapes interaction partner networks on cell membranes.The EMBO journal · 2020Article
- Membrane Compartmentalization and Scaffold Proteins in Leukocyte Migration.Frontiers in cell and developmental biology · 2020Review
- Classes of non-conventional tetraspanins defined by alternative splicing.Scientific reports · 2019Article
- Inhibition of Tetraspanin Functions Impairs Human Papillomavirus and Cytomegalovirus Infections.International journal of molecular sciences · 2018Article
- Stabilization of the CD81 Large Extracellular Loop withPharmaceutics · 2018Article
- Tetraspanin Assemblies in Virus Infection.Frontiers in immunology · 2018Review
- New insights into the tetraspanin Tspan5 using novel monoclonal antibodies.The Journal of biological chemistry · 2017Article
- Tspan2: a tetraspanin protein involved in oligodendrogenesis and cancer metastasis.Biochemical Society transactions · 2017Review
- Tetraspanins Function as Regulators of Cellular Signaling.Frontiers in cell and developmental biology · 2017Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tetraspanins are a superfamily of transmembrane proteins implicated in cellular development, motility, and activation through their interactions with a large range of proteins and with specific membrane microdomains. The complete three-dimensional structure of the tetraspanin CD81 has been predicted by molecular modeling and from the crystallographic structure of the EC2 large extracellular domain. Periodicity of sequence conservation, homology modeling, secondary structure prediction, and protein docking were used. The transmembrane domain appears organized as a four-stranded left-handed coiled coil directly connecting to two helices of the EC2. A smaller extracellular loop EC1 contains a small largely hydrophobic beta-strand that packs in a conserved hydrophobic groove of the EC2. The palmitoylable intracellular N-terminal segment forms an amphipathic membrane-parallel helix. Structural variability occurs mainly in an hypervariable subdomain of the EC2 and in intracellular regions. Therefore, the variable interaction selectivity of tetraspanins originates both from sequence variability within structurally conserved domains and from the occurrence of small structurally variable domains. In CD81 and other tetraspanins, the numerous membrane-exposed aromatic residues are asymmetrically clustered and protrude on one side of the transmembrane domain. This may represent a functional specialization of these two sides for interactions with cholesterol, proteins, or membrane microdomains.
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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.