This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3dpy
From Proteopedia
Contents |
Protein farnesyltransferase complexed with FPP and caged TKCVIM substrate
Template:ABSTRACT PUBMED 18844669
Function
[FNTA_RAT] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity). [FNTB_RAT] Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
About this Structure
3dpy is a 3 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
- DeGraw AJ, Hast MA, Xu J, Mullen D, Beese LS, Barany G, Distefano MD. Caged protein prenyltransferase substrates: tools for understanding protein prenylation. Chem Biol Drug Des. 2008 Sep;72(3):171-81. doi: 10.1111/j.1747-0285.2008.00698.x. PMID:18844669 doi:10.1111/j.1747-0285.2008.00698.x
