Search results for " epolactaene"

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The Binding Mechanism of Epolactaene to Hsp60 Unveiled by in Silico Modelling

2016

Molecular Dynamics (MD) simulations and DFT/MM calculations were performed in order to rationalize available experimental results and to provide structural details on the binding mechanism of Epolactaene (EPO) to the 60 KDa Heat Shock Protein (Hsp60). The available crystal structure of Hsp60 represents the last step of the chaperone folding cycle, while the Hsp60-EPO complex was obtained by using a homology model of Hsp60, in order to simulate a state related to the beginning of the folding cycle (Rs1). The results of MD simulations point out that EPO shows the highest binding affinity for the empty ATP binding site. The presence of ATP opens a channel that allows the entrance of both EPO d…

0301 basic medicineConformational changeanimal structuresStereochemistryProteins · Molecular Dynamics · Density Functional Theory · Heat Shock Proteins · Epolactaene010402 general chemistry01 natural sciences03 medical and health sciencesMolecular dynamicschemistry.chemical_compoundHeat shock proteinHomology modelingBinding siteEpolactaenebiologyChemistrySettore BIO/16 - Anatomia UmanafungiGeneral ChemistrySettore CHIM/06 - Chimica Organica0104 chemical sciencesCrystallography030104 developmental biologyCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaChaperone (protein)biology.protein
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Hsp60 chaperonopathies and chaperonotherapy: targets and agents

2014

Hsp60 (Cpn60) assembles into a tetradecamer that interacts with the co-chaperonin Hsp10 (Cpn10) to assist client polypeptides to fold, but it also has other roles, including participation in pathogenic mechanisms.Hsp60 chaperonopathies are pathological conditions, inherited or acquired, in which the chaperone plays a determinant etiologic-pathogenic role. These diseases justify selection of Hsp60 as a target for developing agents that interfere with its pathogenic effects. We provide information on how to proceed.The information available encourages the development of ways to improve Hsp60 activity (positive chaperonotherapy) when deficient or to block it (negative chaperonotherapy) when pa…

InflammationPharmacologyanimal structuresChaperonin 60biologyProtein ConformationfungiClinical BiochemistryChaperonin 60BioinformaticsAutoimmune Diseasesautoimmunity cancer carboranylphenoxyacetanilide chaperonopathies chaperonotherapy chemical compounds Cpn60 electrophilic compounds epolactaene functional domain GroEL Hsp60 inflammation mizoribine structural domainNeoplasmsChaperone (protein)Expert opinionDrug DiscoveryImmunologybiology.proteinAnimalsHumansMolecular MedicineHSP60Cytokine formationA determinantExpert Opinion on Therapeutic Targets
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