Compensatory and long-range changes in picosecond-nanosecond main-chain dynamics upon complex formation: 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1.

Compensatory and long-range changes in picosecond-nanosecond main-chain dynamics upon complex formation: 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1.

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Structure and function of the intracellular region of the plexin-b1 transmembrane receptor Plexin-B2 negatively regulates macrophage motility, Rac, and Cdc42 activation Insights into Oncogenic Mutations of Plexin-B1 Based on the Solution Structure of the Rho GTPase Binding Domain Large conformational changes in proteins: signaling and other functions.Direct and allosteric inhibition of the FGF2/HSPGs/FGFR1 ternary complex formation by an antiangiogenic, thrombospondin-1-mimic small molecule.A direct coupling between global and internal motions in a single domain protein? MD investigation of extreme scenarios.Structural basis of Rnd1 binding to plexin Rho GTPase binding domains (RBDs)K-Ras at Anionic Membranes: Orientation, Orientation…Orientation. Recent Simulations and Experiments.NMR reveals novel mechanisms of protein activity regulation.Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions.Dissociation of a Dynamic Protein Complex Studied by All-Atom Molecular Simulations.Molecular Dynamics Simulations Reveal Isoform Specific Contact Dynamics between the Plexin Rho GTPase Binding Domain (RBD) and Small Rho GTPases Rac1 and Rnd1.Interactions between PTB RRMs induce slow motions and increase RNA binding affinity.Backbone assignment and secondary structure of Rnd1, an unusual Rho family small GTPase.The insert region of the Rac GTPases is dispensable for activation of superoxide-producing NADPH oxidases.Optimization and stabilization of Rho small GTPase proteins for solution NMR studies: The case of Rnd1.Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions.Discerning intersecting fusion-activation pathways in the Nipah virus using machine learning.Structure and dynamics analysis on plexin-B1 Rho GTPase binding domain as a monomer and dimer.Thermodynamic characterization of two homologous protein complexes: associations of the semaphorin receptor plexin-B1 RhoGTPase binding domain with Rnd1 and active Rac1.Tripping a switch: PDZRhoGEF rgRGS-bound Galpha13.Integrated computational approach to the analysis of NMR relaxation in proteins: application to ps-ns main chain 15N-1H and global dynamics of the Rho GTPase binding domain of plexin-B1.Analysis of 15N-1H NMR relaxation in proteins by a combined experimental and molecular dynamics simulation approach: picosecond-nanosecond dynamics of the Rho GTPase binding domain of plexin-B1 in the dimeric state indicates allosteric pathways.Characterizing Plexin GTPase Interactions Using Gel Filtration, Surface Plasmon Resonance Spectrometry, and Isothermal Titration Calorimetry.

P2860

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P2860

Compensatory and long-range changes in picosecond-nanosecond main-chain dynamics upon complex formation: 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1.

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article científic

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artigo científico

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bilimsel makale

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scientific article published on 04 February 2008

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