Structure of human Rack1 protein at a resolution of 2.45 A.
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Ruiz Carrillo D, Chandrasekaran R, Nilsson M, Cornvik T, Liew CW, Tan SM, Lescar J
Structure of human Rack1 protein at a resolution of 2.45 A.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Aug 1;68(Pt 8):867-72. doi: 10.1107/S1744309112027480. Epub 2012 Jul 26.
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- 22869111 [ View in PubMed]
- Abstract
The crystal structure of human receptor for activated C-kinase 1 (hRack1) protein is reported at 2.45 A resolution. The crystals belongs to space group P4(1)2(1)2, with three molecules per asymmetric unit. The hRack1 structure features a sevenfold beta-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.