2007
Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex
Nolen BJ, Pollard TD. Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex. Molecular Cell 2007, 26: 449-457. PMID: 17499050, PMCID: PMC1997283, DOI: 10.1016/j.molcel.2007.04.017.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesCattleCross-Linking ReagentsGlutaralHumansKineticsMacromolecular SubstancesModels, MolecularNucleotidesProtein ConformationProtein Interaction MappingProtein Structure, TertiaryConceptsArp2/3 complexATP bindingSubdomain 1Actin-family proteinsConformational changesLarge-scale conformational changesActin filament branchesNetwork of interactionsInfluence of nucleotidesActin familyFamily proteinsActin structuresFilament branchesIntrinsic disorderArp3ATPase cycleSteric clashesArp2/3Arp2NucleotidesResiduesComplexesBindingAdenine nucleotidesNew electron density
2006
Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin
Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD. Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin. Cell 2006, 124: 423-435. PMID: 16439214, DOI: 10.1016/j.cell.2005.11.038.Peer-Reviewed Original ResearchConceptsATP hydrolysisTotal internal reflection fluorescence microscopyActin filament polymerizationReflection fluorescence microscopyDiversity of functionsPresence of profilinMammalian forminFormin proteinsFormin mDia1Processive elongationFilament polymerizationForminsActin filamentsBiochemical activityBarbed endsProfilinFluorescence microscopyADP-actinAssembly stepsRecent studiesMDia1Common featureProcessivityElongationProtein