ArticleProteins2009
Structural coupling between FKBP12 and buried water.
Article in Proteins, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 70 citations in OpenAlex.
- OsFKBP12 transduces the sucrose signal from OsNIN8 to the OsTOR pathway in a loosely binding manner for cell division.iScience · 2025Article
- Map conformational landscapes of intrinsically disordered proteins with polymer physics quantities.Biophysical journal · 2024Article
- Propagation of conformational instability in FK506-binding protein FKBP12.Biochimica et biophysica acta. Proteins and proteomics · 2024Article
- Chemical remodeling of a cellular chaperone to target the active state of mutant KRAS.Science (New York, N.Y.) · 2023Article
- Single-molecule fingerprinting of protein-drug interaction using a funneled biological nanopore.Nature communications · 2023Article
- RosettaDDGPrediction for high-throughput mutational scans: From stability to binding.Protein science : a publication of the Protein Society · 2023Article
- Structural features of chloroplast trigger factor determined at 2.6 Å resolution.Acta crystallographica. Section D, Structural biology · 2022Article
- Article
- Environment-Specific Force Field for Intrinsically Disordered and Ordered Proteins.Journal of chemical information and modeling · 2020Article
- Ubiquitylation Directly Induces Fold Destabilization of Proteins.Scientific reports · 2016Article
- Stay Wet, Stay Stable? How Internal Water Helps the Stability of Thermophilic Proteins.The journal of physical chemistry. B · 2015Article
- Role of Internal Water on Protein Thermal Stability: The Case of Homologous G Domains.The journal of physical chemistry. B · 2015Article
- Kinetics of exchange between zero-, one-, and two-hydrogen-bonded states of methyl and ethyl acetate in methanol.The journal of physical chemistry. B · 2015Article
- Conformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design.Current molecular pharmacology · 2015Review
- Article
- Statistical allosteric coupling to the active site indole ring flip equilibria in the FK506-binding domain.Biophysical chemistry · 2014Article
- Structural basis of conformational transitions in the active site and 80's loop in the FK506-binding protein FKBP12.The Biochemical journal · 2014Article
- Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structure-affinity properties of a high-affinity ligand of FKBP12 studied by molecular simulations of a binding intermediate.PloS one · 2014Article
- Analysing the visible conformational substates of the FK506-binding protein FKBP12.The Biochemical journal · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Globular proteins often contain structurally well-resolved internal water molecules. Previously, we reported results from a molecular dynamics study that suggested that buried water (Wat3) may play a role in modulating the structure of the FK506 binding protein-12 (FKBP12) (Park and Saven, Proteins 2005; 60:450-463). In particular, simulations suggested that disrupting a hydrogen bond to Wat3 by mutating E60 to either A or Q would cause a structural perturbation involving the distant W59 side chain, which rotates to a new conformation in response to the mutation. This effectively remodels the ligand-binding pocket, as the side chain in the new conformation is likely to clash with bound FK506. To test whether the protein structure is in effect modulated by the binding of a buried water in the distance, we determined high-resolution (0.92-1.29 A) structures of wild-type FKBP12 and its two mutants (E60A, E60Q) by X-ray crystallography. The structures of mutant FKBP12 show that the ligand-binding pocket is indeed remodeled as predicted by the substitution at position 60, even though the water molecule does not directly interact with any of the amino acids of the binding pocket. Thus, these structures support the view that buried water molecules constitute an integral, noncovalent component of the protein structure. Additionally, this study provides an example in which predictions from molecular dynamics simulations are experimentally validated with atomic precision, thus showing that the structural features of protein-water interactions can be reliably modeled at a molecular level.
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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.