Topic
Ternary complex
About: Ternary complex is a research topic. Over the lifetime, 5107 publications have been published within this topic receiving 188872 citations.
Papers published on a yearly basis
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Papers
TL;DR: In this paper, a ternary complex model was used to fit the data with high accuracy under conditions where the ligand used is either a full or a partial agonist and where the system is altered by the addition of guanine nucleotide or after treatment with group-specific reagents.
1,628 citations
TL;DR: Findings directly link transcriptional activation by the SRE to the growth factor-regulated phosphorylation of an SRE-binding protein to the activity in vivo of the Elk-1 C-terminal region.
1,347 citations
TL;DR: The experimental findings with the mutant receptor cannot be adequately rationalized within the theoretical framework of the Ternary Complex Model, and an extended version of this model that includes an explicit isomerization of the receptor to an active state closely models all the findings for both the mutant and the wild-type receptors.
1,309 citations
TL;DR: The structure of the FRB domain of FRAP clarifies both rapamycin-independent and -dependent effects observed for mutants ofFRAP and its homologs in the family of proteins related to the ataxia-telangiectasia mutant gene product, and it illustrates how a small cell-permeable molecule can mediate protein dimerization.
Abstract: Rapamycin, a potent immunosuppressive agent, binds two proteins: the FK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and the FKBP12-rapamycin-binding (FRB) domain of human FRAP at a resolution of 2.7 angstroms revealed the two proteins bound together as a result of the ability of rapamycin to occupy two different hydrophobic binding pockets simultaneously. The structure shows extensive interactions between rapamycin and both proteins, but fewer interactions between the proteins. The structure of the FRB domain of FRAP clarifies both rapamycin-independent and -dependent effects observed for mutants of FRAP and its homologs in the family of proteins related to the ataxia-telangiectasia mutant gene product, and it illustrates how a small cell-permeable molecule can mediate protein dimerization.
968 citations
TL;DR: The crystal structure at 1.7 Å resolution of the carbohydrate-recognition domain of rat mannose-binding protein complexed with an oligomannose asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds with the carbohydrate ligand.
Abstract: C-type (Ca2+-dependent) animal lectins such as mannose-binding proteins mediate many cell-surface carbohydrate-recognition events. The crystal structure at 1.7 A resolution of the carbohydrate-recognition domain of rat mannose-binding protein complexed with an oligomannose asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds with the carbohydrate ligand. Carbohydrate specificity is determined by a network of coordination and hydrogen bonds that stabilizes the ternary complex of protein, Ca2+ and sugar. Two branches of the oligosaccharide crosslink neighbouring carbohydrate-recognition domains in the crystal, enabling multivalent binding to a single oligosaccharide chain to be visualized directly.
932 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 33 |
| 2024 | 51 |
| 2023 | 91 |
| 2022 | 146 |
| 2021 | 107 |
| 2020 | 113 |