Structural Analysis of the Complex of Human Transthyretin with 3′,5′-Dichlorophenylanthranilic Acid at 1.5 Å Resolution

Structural Analysis of the Complex of Human Transthyretin with 3′,5′-Dichlorophenylanthranilic Acid at 1.5 Å Resolution

Human transthyretin (hTTR) can form amyloid deposits that accumulate in nerves and organs, disrupting cellular function. Molecules such as tafamidis that bind to and stabilize the TTR tetramer can reduce such amyloid formation. Here, we studied the interaction of VCP-6 (2-((3,5-dichlorophenyl)amino)...

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Bibliographic Details
Main Authors: Vivian Cody, Jia Q. Truong, Bruce A. Holdsworth, Jessica K. Holien, Samantha J. Richardson, David K. Chalmers, David J. Craik
Format: Article
Language:English
Published: MDPI AG 2022-10-01
Series:Molecules
Subjects:
human transthyretin
TTR
binding affinity
molecular structure
halogen bonding
Online Access:https://www.mdpi.com/1420-3049/27/21/7206

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https://www.mdpi.com/1420-3049/27/21/7206

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