dc.contributor.authorRuiz Carrillo, David
dc.contributor.authorChandrasekaran, Ramya
dc.contributor.authorNilsson, Martina
dc.contributor.authorCornvik, Tobias Carl
dc.contributor.authorLiew, Chong Wai
dc.contributor.authorTan, Suet Mien
dc.contributor.authorLescar, Julien
dc.date.accessioned2013-02-28T05:40:36Z
dc.date.available2013-02-28T05:40:36Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationRuiz Carrillo, D., Chandrasekaran, R., Nilsson, M., Cornvik, T. C., Liew, C. W., Tan, S. M., et al. (2012). Structure of human Rack1 protein at a resolution of 2.45 Å. Acta crystallographica section F structural biology and crystallization communications, 68(8), 867-872.en_US
dc.identifier.issn1744-3091en_US
dc.identifier.urihttp://hdl.handle.net/10220/9300
dc.description.abstractThe crystal structure of human receptor for activated C-kinase 1 (hRack1) protein is reported at 2.45 Å resolution. The crystals belongs to space group P41212, with three molecules per asymmetric unit. The hRack1 structure features a sevenfold -propeller, with each blade housing a sequence motif that contains a strictly conserved Trp, the indole group of which is embedded between adjacent blades. In blades 1-5 the imidazole group of a His residue is wedged between the side chains of a Ser residue and an Asp residue through two hydrogen bonds. The hRack1 crystal structure forms a starting basis for understanding the remarkable scaffolding properties of this protein.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesActa crystallographica section F structural biology and crystallization communicationsen_US
dc.rights© 2012 International Union of Crystallography. This paper was published in Acta Crystallographica Section F Structural Biology and Crystallization Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [http://dx.doi.org/10.1107/S1744309112027480]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.en_US
dc.subjectDRNTU::Science::Biological sciences::Biochemistry
dc.subjectDRNTU::Science::Chemistry::Crystallography
dc.titleStructure of human Rack1 protein at a resolution of 2.45 Åen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1107/S1744309112027480
dc.description.versionPublished versionen_US


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