ReviewFrontiers in molecular biosciences2020
Structural Perspectives on Extracellular Recognition and Conformational Changes of Several Type-I Transmembrane Receptors.
Review in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 55 citations in OpenAlex.
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- IsoProDB: an integrated map of human protein isoforms for accelerated research.Database : the journal of biological databases and curation · 2026Article
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- Neutron spin echo shows pHLIP is capable of retarding membrane thickness fluctuations.Biochimica et biophysica acta. Biomembranes · 2024Article
- Semaphorin heterodimerization in cis regulates membrane targeting and neocortical wiring.Nature communications · 2024Article
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- A comprehensive analysis of the genetic diversity and environmental adaptability in worldwide Merino and Merino-derived sheep breeds.Genetics, selection, evolution : GSE · 2023Article
- Structural insights into the contactin 1 - neurofascin 155 adhesion complex.Nature communications · 2022Article
- Dawn of a New Era for Membrane Protein Design.Biodesign research · 2022Review
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- BRANEart: Identify Stability Strength and Weakness Regions in Membrane Proteins.Frontiers in bioinformatics · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type-I transmembrane proteins represent a large group of 1,412 proteins in humans with a multitude of functions in cells and tissues. They are characterized by an extracellular, or luminal, N-terminus followed by a single transmembrane helix and a cytosolic C-terminus. The domain composition and structures of the extracellular and intercellular segments differ substantially amongst its members. Most of the type-I transmembrane proteins have roles in cell signaling processes, as ligands or receptors, and in cellular adhesion. The extracellular segment often determines specificity and can control signaling and adhesion. Here we focus on recent structural understanding on how the extracellular segments of several diverse type-I transmembrane proteins engage in interactions and can undergo conformational changes for their function. Interactions at the extracellular side by proteins on the same cell or between cells are enhanced by the transmembrane setting. Extracellular conformational domain rearrangement and structural changes within domains alter the properties of the proteins and are used to regulate signaling events. The combination of structural properties and interactions can support the formation of larger-order assemblies on the membrane surface that are important for cellular adhesion and intercellular signaling.
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Registered trials
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