Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/100793
Title: Structure of human Rack1 protein at a resolution of 2.45 Å
Authors: Lescar, Julien
Cornvik, Tobias Carl
Liew, Chong Wai
Tan, Suet Mien
Ruiz Carrillo, David
Chandrasekaran, Ramya
Nilsson, Martina
Keywords: DRNTU::Science::Biological sciences::Biochemistry
DRNTU::Science::Chemistry::Crystallography
Issue Date: 2012
Source: Ruiz 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.
Series/Report no.: Acta crystallographica section F structural biology and crystallization communications
Abstract: The 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.
URI: https://hdl.handle.net/10356/100793
http://hdl.handle.net/10220/9300
ISSN: 1744-3091
DOI: 10.1107/S1744309112027480
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.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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