Topic
Protein quaternary structure
About: Protein quaternary structure is a research topic. Over the lifetime, 2010 publications have been published within this topic receiving 87086 citations.
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TL;DR: The quaternary structures of these proteins form the basis of a higher level of specificity, where the spacing between individual epitopes of multivalent carbohydrates becomes important, and is of relevance for their effects on the biological activities of cells such as mitogenic responses.
508 citations
TL;DR: A methodology combining time-resolved fluorescence resonance energy transfer (FRET) with snap-tag technology to quantitatively analyze protein-protein interactions at the surface of living cells, in a high throughput–compatible format is described.
Abstract: Cell-surface proteins are important in cell-cell communication. They assemble into heterocomplexes that include different receptors and effectors. Elucidation and manipulation of such protein complexes offers new therapeutic possibilities. We describe a methodology combining time-resolved fluorescence resonance energy transfer (FRET) with snap-tag technology to quantitatively analyze protein-protein interactions at the surface of living cells, in a high throughput-compatible format. Using this approach, we examined whether G protein-coupled receptors (GPCRs) are monomers or assemble into dimers or larger oligomers--a matter of intense debate. We obtained evidence for the oligomeric state of both class A and class C GPCRs. We also observed different quaternary structure of GPCRs for the neurotransmitters glutamate and gamma-aminobutyric acid (GABA): whereas metabotropic glutamate receptors assembled into strict dimers, the GABA(B) receptors spontaneously formed dimers of heterodimers, offering a way to modulate G-protein coupling efficacy. This approach will be useful in systematic analysis of cell-surface protein interaction in living cells.
501 citations
TL;DR: Wang et al. as discussed by the authors investigated the oligomeric state of α-syn in mouse, rat, and human brains and showed that both human and rodent αsyn expressed in the central nervous system exist predominantly as an unfolded monomer.
493 citations
TL;DR: Detailed investigation of the higher-order structure of 16 S ribosomal RNA and extensive protection of conserved, unpaired adenines upon formation of 30 S subunits suggests that they play a special role in the assembly process, possibly providing signals for protein recognition.
484 citations
TL;DR: Key questions that remain to be addressed effectively include the prevalence and relevance of these in native tissues and the implications of heterodimerization for pharmacology and, potentially, for drug design.
Abstract: It is now generally accepted that G protein-coupled receptors (GPCRs) can exist as dimers or as part of larger oligomeric complexes. Increasing evidence suggests that a dimer is the minimal functional structure, but considerable variation exists between reports of the effects of agonist ligands on quaternary structure. Many studies have intimated the existence of heterodimeric GPCR pairings. Key questions that remain to be addressed effectively include the prevalence and relevance of these in native tissues and the implications of heterodimerization for pharmacology and, potentially, for drug design.
480 citations