Open AccessStructure of human Rack1 protein at a resolution of 2.45 Å
Author(s) -
Ruiz Carrillo David,
Chandrasekaran Ramya,
Nilsson Martina,
Cornvik Tobias,
Liew Chong Wai,
Tan Suet Mien,
Lescar Julien
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112027480
Subject(s) - residue (chemistry) , crystal structure , hydrogen bond , crystallography , imidazole , molecule , stereochemistry , chemistry , biochemistry , organic chemistry
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 P 4 1 2 1 2, 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.