ArticleBMC structural biology2013
An analysis of oligomerization interfaces in transmembrane proteins.
Article in BMC structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
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- Deep transfer learning for inter-chain contact predictions of transmembrane protein complexes.Nature communications · 2023Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Ion mobility-mass spectrometry reveals the role of peripheral myelin protein dimers in peripheral neuropathy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- MENSAdb: a thorough structural analysis of membrane protein dimers.Database : the journal of biological databases and curation · 2021Article
- Getting to know each other: PPIMem, a novel approach for predicting transmembrane protein-protein complexes.Computational and structural biotechnology journal · 2021Article
- Mcl-1 and Bok transmembrane domains: Unexpected players in the modulation of apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The mitochondrial ADP/ATP carrier exists and functions as a monomer.Biochemical Society transactions · 2020Review
- In vitro assembly of Haemophilus influenzae adhesin transmembrane domain and studies on the electrostatic repulsion at the interface.Biophysical reviews · 2019Review
- Distinguishing crystallographic from biological interfaces in protein complexes: role of intermolecular contacts and energetics for classification.BMC bioinformatics · 2018Article
- Crystal structure of rhodopsin in complex with a mini-GScience advances · 2018Article
- Assessment of protein assembly prediction in CASP12.Proteins · 2018Article
- Crystal structures of theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Recent Advances and Applications of Molecular Docking to G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2017Review
- Article
- Apelin receptor homodimer-oligomers revealed by single-molecule imaging and novel G protein-dependent signaling.Scientific reports · 2017Article
- Accurate Prediction of Contact Numbers for Multi-Spanning Helical Membrane Proteins.Journal of chemical information and modeling · 2016Article
- A structural dissection of large protein-protein crystal packing contacts.Scientific reports · 2015Article
- The Hedgehog pathway: role in cell differentiation, polarity and proliferation.Archives of toxicology · 2015Review
- A PDB-wide, evolution-based assessment of protein-protein interfaces.BMC structural biology · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe amount of transmembrane protein (TM) structures solved to date is now large enough to attempt large scale analyses. In particular, extensive studies of oligomeric interfaces in the transmembrane region are now possible.
resultsWe have compiled the first fully comprehensive set of validated transmembrane protein interfaces in order to study their features and assess what differentiates them from their soluble counterparts.
conclusionsThe general features of TM interfaces do not differ much from those of soluble proteins: they are large, tightly packed and possess many interface core residues. In our set, membrane lipids were not found to significantly mediate protein-protein interfaces. Although no G protein-coupled receptor (GPCR) was included in the validated set, we analyzed the crystallographic dimerization interfaces proposed in the literature. We found that the putative dimer interfaces proposed for class A GPCRs do not show the usual patterns of stable biological interfaces, neither in terms of evolution nor of packing, thus they likely correspond to crystal interfaces. We cannot however rule out the possibility that they constitute transient or weak interfaces. In contrast we do observe a clear signature of biological interface for the proposed dimer of the class F human Smoothened receptor.
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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.