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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 cell survival, and inhibition of farnesyl pyropho...

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Authors


Kavanagh, Kathryn L More by this author
Dunford, James E More by this author
Bunkoczi, Gabor More by this author
Russell, R Graham G More by this author
Oppermann, Udo More by this author
Journal:
The Journal of biological chemistry
Volume:
281
Issue:
31
Pages:
22004-12
Publication date:
2006-08-04
ISSN:
0021-9258
URN:
uuid:314b52e6-047b-4635-a61b-ea6d1c710a63
Local pid:
SGC:16698791

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