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Structure of human Rack1 protein at a resolution of 2.45?A.

ABSTRACT: 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 P4(1)2(1)2, 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.

SUBMITTER: Ruiz Carrillo D

PROVIDER: S-EPMC3412762 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Structure of human Rack1 protein at a resolution of 2.45 Å.

Ruiz Carrillo David D Chandrasekaran Ramya R Nilsson Martina M Cornvik Tobias T Liew Chong Wai CW Tan Suet Mien SM Lescar Julien J

Acta crystallographica. Section F, Structural biology and crystallization communications 20120726 Pt 8

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 P4(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 r ...[more]

PMID: 22869111

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