ArticleBiophysical journal2005
Anesthetic interaction with ketosteroid isomerase: insights from molecular dynamics simulations.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- The role of structured water in mediating general anesthetic action on alpha4beta2 nAChR.Physical chemistry chemical physics : PCCP · 2010Article
- Sevoflurane binds and allosterically blocks integrin lymphocyte function-associated antigen-1.Anesthesiology · 2010Article
- Unresponsive correlated motion in alpha7 nAChR to halothane binding explains its functional insensitivity to volatile anesthetics.The journal of physical chemistry. B · 2010Article
- General anesthetic binding to neuronal alpha4beta2 nicotinic acetylcholine receptor and its effects on global dynamics.The journal of physical chemistry. B · 2009Article
- In vivo measurement of protein functional changes.International journal of biological sciences · 2009Article
- The volatile anesthetic isoflurane perturbs conformational activation of integrin LFA-1 by binding to the allosteric regulatory cavity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008Article
- Interaction of anesthetics with open and closed conformations of a potassium channel studied via molecular dynamics and normal mode analysis.Biophysical journal · 2008Article
- Four-alpha-helix bundle with designed anesthetic binding pockets. Part I: structural and dynamical analyses.Biophysical journal · 2008Article
- Four-alpha-helix bundle with designed anesthetic binding pockets. Part II: halothane effects on structure and dynamics.Biophysical journal · 2008Article
- Dynamics of firefly luciferase inhibition by general anesthetics: Gaussian and anisotropic network analyses.Biophysical journal · 2007Article
- Prediction of volatile anesthetic binding sites in proteins.Biophysical journal · 2006Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nature and the sites of interactions between anesthetic halothane and homodimeric Delta5-3-ketosteroid isomerase (KSI) are characterized by flexible ligand docking and confirmed by 1H-15N NMR. The dynamics consequence of halothane interaction and the implication of the dynamic changes to KSI function are studied by multiple 5-ns molecular dynamics simulations in the presence and absence of halothane. Both docking and MD simulations show that halothane prefer the amphiphilic dimeric interface to the hydrophobic active site of KSI. Halothane occupancy at the dimer interface disrupted the intersubunit hydrogen bonding formed either directly through side chains of polar residues or indirectly through the mediation of the interfacial water molecules. Moreover, in the presence of halothane, the exchange rate of the bound waters with bulk water was increased. Halothane perturbation to the dimer interface affected the overall flexibility of the active site. This action is likely to contribute to the halothane-induced reduction of the KSI activity. The allosteric halothane modulation of the dynamics-function relationship of KSI without direct competition at the enzymatic active sites may be generalized to offer a unifying explanation of anesthetic action on a diverse range of multidomain neuronal proteins that are potentially relevant to clinical general anesthesia.
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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.