Structural highlights
Publication Abstract from PubMed
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.
Structure of human Rack1 protein at a resolution of 2.45 A.,Ruiz Carrillo D, Chandrasekaran R, Nilsson M, Cornvik T, Liew CW, Tan SM, Lescar J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Aug 1;68(Pt 8):867-72., Epub 2012 Jul 26. PMID:22869111[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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., Epub 2012 Jul 26. PMID:22869111 doi:10.1107/S1744309112027480
