4r3m
From Proteopedia
Crystal structure of Human Hsp90 with JR9
Structural highlights
Function[HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.[1] [2] Publication Abstract from PubMedUsing a 2,3-diamino pyrazine substrate and yttrium triflate catalyst, various 2-alkyl and aryl substituted 3,8-diaminoimidazo[1,2-a]pyrazines were efficiently prepared through Groebke-Blackburn-Bienayme MCR. In particular, a novel 2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazine structure was prepared exclusively with this new method and was found to have moderate Hsp90 inhibitory activity. A crystalline complex with N-terminus ATP domain of Hsp90 and one of the new Hsp90 inhibitors was also obtained to elucidate the origin of activity of 2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazines. Multi-substituted 8-aminoimidazo[1,2-a]pyrazines by Groebke-Blackburn-Bienayme reaction and their Hsp90 inhibitory activity.,Ren J, Yang M, Liu H, Cao D, Chen D, Li J, Tang L, He J, Chen YL, Geng M, Xiong B, Shen J Org Biomol Chem. 2015 Feb 7;13(5):1531-5. doi: 10.1039/c4ob01865f. PMID:25490978[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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