Structure of human Rack1 protein at a resolution of 2.45 Å
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 tha...
Main Authors: | , , , , , , |
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Format: | Journal Article |
Language: | English |
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2013
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Online Access: | https://hdl.handle.net/10356/100793 http://hdl.handle.net/10220/9300 |
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author | Lescar, Julien Cornvik, Tobias Carl Liew, Chong Wai Tan, Suet Mien Ruiz Carrillo, David Chandrasekaran, Ramya Nilsson, Martina |
author2 | School of Biological Sciences |
author_facet | School of Biological Sciences Lescar, Julien Cornvik, Tobias Carl Liew, Chong Wai Tan, Suet Mien Ruiz Carrillo, David Chandrasekaran, Ramya Nilsson, Martina |
author_sort | Lescar, Julien |
collection | NTU |
description | 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. |
first_indexed | 2024-10-01T06:15:20Z |
format | Journal Article |
id | ntu-10356/100793 |
institution | Nanyang Technological University |
language | English |
last_indexed | 2024-10-01T06:15:20Z |
publishDate | 2013 |
record_format | dspace |
spelling | ntu-10356/1007932023-02-28T17:04:52Z Structure of human Rack1 protein at a resolution of 2.45 Å Lescar, Julien Cornvik, Tobias Carl Liew, Chong Wai Tan, Suet Mien Ruiz Carrillo, David Chandrasekaran, Ramya Nilsson, Martina School of Biological Sciences DRNTU::Science::Biological sciences::Biochemistry DRNTU::Science::Chemistry::Crystallography 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. Published version 2013-02-28T05:40:36Z 2019-12-06T20:28:22Z 2013-02-28T05:40:36Z 2019-12-06T20:28:22Z 2012 2012 Journal Article 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. 1744-3091 https://hdl.handle.net/10356/100793 http://hdl.handle.net/10220/9300 10.1107/S1744309112027480 22869111 en Acta crystallographica section F structural biology and crystallization communications © 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. application/pdf |
spellingShingle | DRNTU::Science::Biological sciences::Biochemistry DRNTU::Science::Chemistry::Crystallography Lescar, Julien Cornvik, Tobias Carl Liew, Chong Wai Tan, Suet Mien Ruiz Carrillo, David Chandrasekaran, Ramya Nilsson, Martina Structure of human Rack1 protein at a resolution of 2.45 Å |
title | Structure of human Rack1 protein at a resolution of 2.45 Å |
title_full | Structure of human Rack1 protein at a resolution of 2.45 Å |
title_fullStr | Structure of human Rack1 protein at a resolution of 2.45 Å |
title_full_unstemmed | Structure of human Rack1 protein at a resolution of 2.45 Å |
title_short | Structure of human Rack1 protein at a resolution of 2.45 Å |
title_sort | structure of human rack1 protein at a resolution of 2 45 a |
topic | DRNTU::Science::Biological sciences::Biochemistry DRNTU::Science::Chemistry::Crystallography |
url | https://hdl.handle.net/10356/100793 http://hdl.handle.net/10220/9300 |
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