Structure of human Rack1 protein at a resolution of 2.45 Å

• Main Authors: Lescar, Julien, Cornvik, Tobias Carl, Liew, Chong Wai, Tan, Suet Mien, Ruiz Carrillo, David, Chandrasekaran, Ramya, Nilsson, Martina
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2013
• Subjects: DRNTU::Science::Biological sciences::Biochemistry; DRNTU::Science::Chemistry::Crystallography
• Online Access: https://hdl.handle.net/10356/100793; http://hdl.handle.net/10220/9300
• Institution: Nanyang Technological University

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.