Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms9681
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dc.titleAn in cellulo-derived structure of PAK4 in complex with its inhibitor Inka1
dc.contributor.authorBaskaran, Y
dc.contributor.authorAng, K.C
dc.contributor.authorAnekal, P.V
dc.contributor.authorChan, W.L
dc.contributor.authorGrimes, J.M
dc.contributor.authorManser, E
dc.contributor.authorRobinson, R.C
dc.date.accessioned2020-09-10T01:46:48Z
dc.date.available2020-09-10T01:46:48Z
dc.date.issued2015
dc.identifier.citationBaskaran, Y, Ang, K.C, Anekal, P.V, Chan, W.L, Grimes, J.M, Manser, E, Robinson, R.C (2015). An in cellulo-derived structure of PAK4 in complex with its inhibitor Inka1. Nature Communications 6 : 8681. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms9681
dc.identifier.issn20411723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175462
dc.description.abstractPAK4 is a metazoan-specific kinase acting downstream of Cdc42. Here we describe the structure of human PAK4 in complex with Inka1, a potent endogenous kinase inhibitor. Using single mammalian cells containing crystals 50 ?m in length, we have determined the in cellulo crystal structure at 2.95 Å resolution, which reveals the details of how the PAK4 catalytic domain binds cellular ATP and the Inka1 inhibitor. The crystal lattice consists only of PAK4-PAK4 contacts, which form a hexagonal array with channels of 80 Å in diameter that run the length of the crystal. The crystal accommodates a variety of other proteins when fused to the kinase inhibitor. Inka1-GFP was used to monitor the process crystal formation in living cells. Similar derivatives of Inka1 will allow us to study the effects of PAK4 inhibition in cells and model organisms, to allow better validation of therapeutic agents targeting PAK4. © 2015 Macmillan Publishers Limited. All rights reserved.
dc.publisherNature Publishing Group
dc.sourceUnpaywall 20200831
dc.subjectadenosine triphosphate
dc.subjectInka1 protein
dc.subjectp21 activated kinase 4
dc.subjectphosphotransferase inhibitor
dc.subjectunclassified drug
dc.subjectadenosine triphosphate
dc.subjectInka protein, human
dc.subjectp21 activated kinase
dc.subjectPAK4 protein, human
dc.subjectprotein binding
dc.subjectsignal peptide
dc.subjectcells and cell components
dc.subjectcrystal structure
dc.subjectenzyme activity
dc.subjectinhibitor
dc.subjectmammal
dc.subjectmetazoan
dc.subjectprotein
dc.subjectanimal cell
dc.subjectArticle
dc.subjectcontrolled study
dc.subjectcrystal structure
dc.subjectenzyme active site
dc.subjecthuman
dc.subjecthuman cell
dc.subjectnonhuman
dc.subjectprotein binding
dc.subjectprotein structure
dc.subjectanimal
dc.subjectchemistry
dc.subjectChlorocebus aethiops
dc.subjectconfocal microscopy
dc.subjectCOS cell line
dc.subjectcrystallization
dc.subjectEscherichia coli
dc.subjectHEK293 cell line
dc.subjectHeLa cell line
dc.subjectimmunoprecipitation
dc.subjectin vitro study
dc.subjectmetabolism
dc.subjectprotein tertiary structure
dc.subjecttumor cell line
dc.subjectX ray crystallography
dc.subjectMammalia
dc.subjectMetazoa
dc.subjectAdenosine Triphosphate
dc.subjectAnimals
dc.subjectCatalytic Domain
dc.subjectCell Line, Tumor
dc.subjectCercopithecus aethiops
dc.subjectCOS Cells
dc.subjectCrystallization
dc.subjectCrystallography, X-Ray
dc.subjectEscherichia coli
dc.subjectHEK293 Cells
dc.subjectHeLa Cells
dc.subjectHumans
dc.subjectImmunoprecipitation
dc.subjectIn Vitro Techniques
dc.subjectIntracellular Signaling Peptides and Proteins
dc.subjectMicroscopy, Confocal
dc.subjectp21-Activated Kinases
dc.subjectProtein Binding
dc.subjectProtein Structure, Tertiary
dc.typeArticle
dc.contributor.departmentDEPT OF PHARMACOLOGY
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.description.doi10.1038/ncomms9681
dc.description.sourcetitleNature Communications
dc.description.volume6
dc.description.page8681
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