6LUR

Human PUF60 UHM domain (thioredoxin fusion) in complex with a small molecule binder

Summary for 6LUR

• Entry DOI: 10.2210/pdb6lur/pdb
• Descriptor: Thioredoxin 1,Poly(U)-binding-splicing factor PUF60, 4-[2-[4-(aminomethyl)phenyl]phenyl]piperazin-2-one (3 entities in total)
• Functional Keywords: splicing factor, splicing
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 8
• Total formula weight: 199626.26

Authors

Takahashi, M.,Hanzawa, H. (deposition date: 2020-01-30, release date: 2020-04-29, Last modification date: 2024-10-23)

Primary citation

Hanzawa, H.,Shimada, T.,Takahashi, M.,Takahashi, H.
Revisiting biomolecular NMR spectroscopy for promoting small-molecule drug discovery.
J.Biomol.Nmr, 74:501-508, 2020

PubMed Abstract: Recently, there has been increasing interest in new modalities such as therapeutic antibodies and gene therapy at a number of pharmaceutical companies. Moreover, in small-molecule drug discovery at such companies, efforts have focused on hard-to-drug targets such as inhibiting protein-protein interactions. Biomolecular NMR spectroscopy has been used in drug discovery in a variety of ways, such as for the reliable detection of binding and providing three-dimensional structural information for structure-based drug design. The advantages of using NMR spectroscopy have been known for decades (Jahnke in J Biomol NMR 39:87-90, (2007); Gossert and Jahnke in Prog Nucl Magn Reson Spectrosc 97:82-125, (2016)). For tackling hard-to-drug targets and increasing the success in discovering drug molecules, in-depth analysis of drug-target protein interactions performed by biophysical methods will be more and more essential. Here, we review the advantages of NMR spectroscopy as a key technology of biophysical methods and also discuss issues such as using cutting-edge NMR spectrometers and increasing the demand of utilizing conformational dynamics information for promoting small-molecule drug discovery.

PubMed: 32306215
DOI: 10.1007/s10858-020-00314-0

Experimental method

X-RAY DIFFRACTION (2 Å)