4AOW

Crystal structure of the human Rack1 protein at a resolution of 2.45 angstrom

Summary for 4AOW

• Entry DOI: 10.2210/pdb4aow/pdb
• Descriptor: GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-2-LIKE 1, GLYCEROL (3 entities in total)
• Functional Keywords: receptor, wd-repeat, beta-propeller
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cell membrane; Peripheral membrane protein: P63244
• Total number of polymer chains: 3
• Total formula weight: 113600.95

Authors

Ruiz Carrillo, D.,Chandrasekaran, R.,Nilsson, M.,Cornvick, T.,Liew, C.W.,Tan, S.M.,Lescar, J. (deposition date: 2012-03-30, release date: 2012-08-08, Last modification date: 2023-12-20)

Primary citation

Ruiz Carrillo, D.,Chandrasekaran, R.,Nilsson, M.,Cornvik, T.,Liew, C.W.,Tan, S.M.,Lescar, J.
Structure of Human Rack1 Protein at a Resolution of 2.45 A.
Acta Crystallogr.,Sect.F, 68:867-, 2012

PubMed 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 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.

PubMed: 22869111
DOI: 10.1107/S1744309112027480

Experimental method

X-RAY DIFFRACTION (2.45 Å)