Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
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NAD(+)-dependent formate dehydrogenaseStructure-activity relationships of Bacillus cereus and Bacillus anthracis dihydrofolate reductase: toward the identification of new potent drug leadsStructure in an extreme environment: NMR at high saltExplaining an Unusually Fast Parasitic Enzyme: Folate Tail-Binding Residues Dictate Substrate Positioning and Catalysis in Cryptosporidium hominis Thymidylate Synthase † ‡NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic InteractionsDivergent evolution of protein conformational dynamics in dihydrofolate reductase.Probing the Electrostatics of Active Site Microenvironments along the Catalytic Cycle for Escherichia coli Dihydrofolate ReductaseDissecting virulence pathways of Mycobacterium tuberculosis through protein-protein association.Keep on moving: discovering and perturbing the conformational dynamics of enzymesTesting the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded formsMolecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: relative stabilities in experiment and simulationsStructure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complexProtein rethreading: A novel approach to protein design.Mining electron density for functionally relevant protein polysterism in crystal structures.Geofold: topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability.Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.Aspects of Weak Interactions between Folate and Glycine Betaine.Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.Effects of fluorine substitution on the structure and dynamics of complexes of dihydrofolate reductase (Escherichia coli).pH-dependent conformational changes in Escherichia coli dihydrofolate reductase revealed by Raman difference spectroscopyRole of water in the catalytic cycle of E. coli dihydrofolate reductase.Ligand binding modulates the mechanical stability of dihydrofolate reductase.Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate.Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensembleFully Flexible Docking of Medium Sized Ligand Libraries with RosettaLigand.Searching sequence space: two different approaches to dihydrofolate reductase catalysis.An active site rearrangement within the Tetrahymena group I ribozyme releases nonproductive interactions and allows formation of catalytic interactions.Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments.Methotrexate resistance in an in vivo mouse tumor due to a non-active-site dihydrofolate reductase mutation.Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle.Generation of a flexible loop structural ensemble and its application to induced-fit structural changes following ligand binding.Systematic alanine insertion reveals the essential regions that encode structure formation and activity of dihydrofolate reductase.Site specific polarization transfer from a hyperpolarized ligand of dihydrofolate reductase.Linking protein motion to enzyme catalysis.Identification of amino acids required for the functional up-regulation of human dihydrofolate reductase protein in response to antifolate Treatment.Comparative hydrogen-deuterium exchange for a mesophilic vs thermophilic dihydrofolate reductase at 25 °C: identification of a single active site region with enhanced flexibility in the mesophilic protein.Extension and limits of the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.Targeting nuclear thymidylate biosynthesis.Detergent-induced conformational changes of Humicola lanuginosa lipase studied by fluorescence spectroscopy.Movable lobes and flexible loops in proteins. Structural deformations that control biochemical activity.
P2860
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P2860
Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
description
1991 nî lūn-bûn
@nan
1991 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Crystal structure of unligande ...... s and cooperativity in binding
@ast
Crystal structure of unligande ...... s and cooperativity in binding
@en
Crystal structure of unligande ...... s and cooperativity in binding
@nl
type
label
Crystal structure of unligande ...... s and cooperativity in binding
@ast
Crystal structure of unligande ...... s and cooperativity in binding
@en
Crystal structure of unligande ...... s and cooperativity in binding
@nl
prefLabel
Crystal structure of unligande ...... s and cooperativity in binding
@ast
Crystal structure of unligande ...... s and cooperativity in binding
@en
Crystal structure of unligande ...... s and cooperativity in binding
@nl
P3181
P356
P1433
P1476
Crystal structure of unligande ...... s and cooperativity in binding
@en
P2093
P304
P3181
P356
10.1021/BI00222A028
P407
P577
1991-02-26T00:00:00Z