Structure of human Rack1 protein at a resolution of 2.45 Å

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 68; no. 8; pp. 867 - 872
• Main Authors: Ruiz Carrillo, David, Chandrasekaran, Ramya, Nilsson, Martina, Cornvik, Tobias, Liew, Chong Wai, Tan, Suet Mien, Lescar, Julien
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-08-2012; Wiley Subscription Services, Inc
• Subjects: Amino Acid Sequence; Crystal structure; Crystallography, X-Ray; GTP-Binding Proteins - chemistry; Humans; Models, Molecular; Molecular Sequence Data; Neoplasm Proteins - chemistry; protein kinase C; Protein Structure, Quaternary; Protein Structure, Tertiary; Proteins; Rack1; Receptors for Activated C Kinase; Receptors, Cell Surface - chemistry; Sequence Alignment; Sequence Homology, Amino Acid; Structural Communications; Structural Homology, Protein; WD repeat; β-propeller
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309112027480

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 β‐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.