The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding.
|Abstract||Modification of GTPases with isoprenoid molecules derived from geranylgeranyl pyrophosphate or farnesyl pyrophosphate is an essential requisite for cellular signaling pathways. The synthesis of these isoprenoids proceeds in mammals through the mevalonate pathway, and the final steps in the synthesis are catalyzed by the related enzymes farnesyl pyrophosphate synthase and geranylgeranyl pyrophosphate synthase. Both enzymes play crucial roles in ce ... [truncated at 450 characters in length]|
|Author||Kavanagh, Kathryn L; Dunford, James E; Bunkoczi, Gabor; et al|
|Subject||Crystallization Crystallography, X-Ray Dimerization Enzyme Inhibitors Feedback, Physiological Geranylgeranyl-Diphosphate Geranylgeranyltransferase Humans Kinetics Molecular Motor Proteins Protein Binding Protein Conformation antagonists and inhibitors chemistry chemistry|