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    p97, an abundant hexameric ATPase of the AAA family, is involved in homotypic membrane fusion. It is thought to disassemble SNARE complexes formed during the process of membrane fusion. Two structures have been reported: a crystal structure of the N-terminal and D1 ATPase domains of murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 A resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and that the N domain is flexible. A comparison with NSF D2 (ATP complex) reveals possible conformational changes induced by ATP hydrolysis.


    Catalog No. Name Description
    GY02524 Special NMS-873 NMS-873 is a potent, selective allosteric VCP/p97 inhibitor with IC50 value of 30 nM.
    GY02030 ML241 HCl ML241 hydrochloride is a potent p97 inhibitor, inhibiting p97 ATPase with IC50 value of 100 nM.
    GY02406 ML240 ML240 is a selective, ATP-competitive p97 inhibitor with IC50 values of 100 nM.
    GY02597 NMS-859 NMS-859 is a potent and specific small molecule covalent inhibitor of the ATPase VCP/p97 (IC50 ~0.37 μM), identified by high-throughput screening.
    GY02818 DBeQ DBeQ(JRF-12) is a selective, potent, reversible, and ATP-competitive p97 inhibitor with IC50 of 1.5 μM.