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3G8E

Crystal Structure of Rattus norvegicus Visfatin/PBEF/Nampt in Complex with an FK866-based inhibitor

Summary for 3G8E
Entry DOI10.2210/pdb3g8e/pdb
Related2G96 2G97
DescriptorNicotinamide phosphoribosyltransferase, 3-[(1E)-3-oxo-3-({4-[1-(phenylcarbonyl)piperidin-4-yl]butyl}amino)prop-1-en-1-yl]-1-beta-D-ribofuranosylpyridinium (2 entities in total)
Functional Keywordsprotein-ligand complex, is001, cytoplasm, glycosyltransferase, nucleus, phosphoprotein, pyridine nucleotide biosynthesis, transferase
Biological sourceRattus norvegicus (rat)
Cellular locationCytoplasm: Q80Z29
Total number of polymer chains2
Total formula weight112074.63
Authors
Kang, G.B.,Bae, M.H.,Kim, M.K.,Im, I.,Kim, Y.C.,Eom, S.H. (deposition date: 2009-02-12, release date: 2009-08-18, Last modification date: 2023-11-01)
Primary citationKang, G.B.,Bae, M.H.,Kim, M.K.,Im, I.,Kim, Y.C.,Eom, S.H.
Crystal structure of Rattus norvegicus Visfatin/PBEF/Nampt in complex with an FK866-based inhibitor
Mol.Cells, 27:667-671, 2009
Cited by
PubMed Abstract: Visfatin (Nampt/PBEF) plays a pivotal role in the salvage pathway for NAD(+) biosynthesis. Its potent inhibitor, FK866, causes cellular NAD(+) levels to decline, thereby inducing apoptosis in tumor cells. In an effort to improve the solubility and binding interactions of FK866, we designed and synthesized IS001, in which a ribose group is attached to the FK866 pyridyl ring. Here, we report the crystal structure of rat visfatin in complex with IS001. Like FK866, IS001 is positioned at the dimer interface, and all of the residues that interact with IS001 are involved in hydrophobic or pi-pi-stacking interactions. However, we were unable to detect any strong interactions between the added ribose ring of IS001 and visfatin, which implies that a bulkier modifying group is necessary for a tight interaction. This study provides additional structure-based information needed to optimize the design of visfatin inhibitors.
PubMed: 19533035
DOI: 10.1007/s10059-009-0088-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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