Structural highlights
Function
GRP75_HUMAN Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone.
Publication Abstract from PubMed
Our early efforts to find a covalent inhibitor of mortalin, a member of the 70 kD heat shock protein (Hsp70) family, led us to solve the structure of the mortalin nucleotide-binding domain (NBD) in complex with N6-propargyladenosine-5'-diphosphate. The acquired structure emphasizes the ability of the nucleotide-binding pocket to accommodate modified ADP compounds. A library of ADP analogues modified at either the 2- or N6-positions of adenosine were screened against the mortalin-NBD. Competitive inhibition and binding assays of the analogues demonstrate that modifications at the 2- or N6-positions have potential to bind and inhibit mortalin uniquely compared to other Hsp70 homologs, and that modifications at the 2-position confer the greatest selectivity in binding and inhibition of the mortalin-NBD. This article is protected by copyright. All rights reserved.
2- and N6-Functionalized Adenosine-5'-diphosphate Analogues for the Inhibition of Mortalin.,Moseng MA, Nix JC, Page RC FEBS Lett. 2019 Jun 8. doi: 10.1002/1873-3468.13475. PMID:31177526[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Moseng MA, Nix JC, Page RC. 2- and N6-Functionalized Adenosine-5'-diphosphate Analogues for the Inhibition of Mortalin. FEBS Lett. 2019 Jun 8. doi: 10.1002/1873-3468.13475. PMID:31177526 doi:http://dx.doi.org/10.1002/1873-3468.13475
