ArticleProtein science : a publication of the Protein Society2009
Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed.
- Tracking Copper sensing operon Repressor (CsoR) oligomerization in solution using Electron Paramagnetic Resonance spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- Shifting the substrate scope of dimeric pyranose oxidase from monosaccharide to glycoside preference through oligomeric state modification.The FEBS journal · 2025Article
- Molecular Modeling of Single- and Double-Hydrocarbon-Stapled Coiled-Coil Inhibitors against Bcr-Abl: Toward a Treatment Strategy for CML.The journal of physical chemistry. B · 2024Article
- Evidence of direct interaction between cisplatin and the caspase-cleaved prostate apoptosis response-4 tumor suppressor.Protein science : a publication of the Protein Society · 2024Article
- An Effective Computational Method for Predicting Self-Interacting Proteins Based on VGGNet Convolutional Neural Network and Gray-Level Co-occurrence Matrix.Evolutionary bioinformatics online · 2024Article
- Computational Modeling of Stapled Coiled-Coil Inhibitors Against Bcr-Abl: Toward a Treatment Strategy for CML.bioRxiv : the preprint server for biology · 2023Article
- Robust and accurate prediction of self-interacting proteins from protein sequence information by exploiting weighted sparse representation based classifier.BMC bioinformatics · 2022Article
- Concentration- and pH-Dependent Oligomerization of the Thrombin-Derived C-Terminal Peptide TCP-25.Biomolecules · 2020Article
- Structural Analysis of the Glycoprotein Complex Avidin by Tandem-Trapped Ion Mobility Spectrometry-Mass Spectrometry (Tandem-TIMS/MS).Analytical chemistry · 2020Article
- Predicting Self-Interacting Proteins Using a Recurrent Neural Network and Protein Evolutionary Information.Evolutionary bioinformatics online · 2020Article
- Prediction of Self-Interacting Proteins from Protein Sequence Information Based on Random Projection Model and Fast Fourier Transform.International journal of molecular sciences · 2019Article
- Prediction of protein self-interactions using stacked long short-term memory from protein sequences information.BMC systems biology · 2018Article
- Computational methods using weighed-extreme learning machine to predict protein self-interactions with protein evolutionary information.Journal of cheminformatics · 2017Article
- Composite structural motifs of binding sites for delineating biological functions of proteins.PloS one · 2012Article
- Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization.Physical biology · 2011Review
- Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Functional states of homooligomers: insights from the evolution of glycosyltransferases.Journal of molecular biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transferases and hydrolases catalyze different chemical reactions and express different dynamic responses upon ligand binding. To insulate the ligand molecule from the surrounding water, transferases bury it inside the protein by closing the cleft, while hydrolases undergo a small conformational change and leave the ligand molecule exposed to the solvent. Despite these distinct ligand-binding modes, some transferases and hydrolases are homologous. To clarify how such different catalytic modes are possible with the same scaffold, we examined the solvent accessibility of ligand molecules for 15 SCOP superfamilies, each containing both transferase and hydrolase catalytic domains. In contrast to hydrolases, we found that nine superfamilies of transferases use two major strategies, oligomerization and domain fusion, to insulate the ligand molecules. The subunits and domains that were recruited by the transferases often act as a cover for the ligand molecule. The other strategies adopted by transferases to insulate the ligand molecule are the relocation of catalytic sites, the rearrangement of secondary structure elements, and the insertion of peripheral regions. These findings provide insights into how proteins have evolved and acquired distinct functions with a limited number of scaffolds.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.