TY - JOUR
T1 - PLBD
T2 - protein-ligand binding database of thermodynamic and kinetic intrinsic parameters
AU - Lingė, Darius
AU - Gedgaudas, Marius
AU - Merkys, Andrius
AU - Petrauskas, Vytautas
AU - Vaitkus, Antanas
AU - Grybauskas, Algirdas
AU - Paketurytė, Vaida
AU - Zubrienė, Asta
AU - Zakšauskas, Audrius
AU - Mickevičiūtė, Aurelija
AU - Smirnovienė, Joana
AU - Baranauskienė, Lina
AU - Crossed D sign apkauskaitė, Edita
AU - Dudutienė, Virginija
AU - Urniežius, Ernestas
AU - Konovalovas, Aleksandras
AU - Kazlauskas, Egidijus
AU - Shubin, Kirill
AU - Schiöth, Helgi B.
AU - Chen, Wen Yih
AU - Ladbury, John E.
AU - Gražulis, Saulius
AU - Matulis, Daumantas
N1 - Publisher Copyright:
© 2023 The Author(s). Published by Oxford University Press.
PY - 2023
Y1 - 2023
N2 - We introduce a protein-ligand binding database (PLBD) that presents thermodynamic and kinetic data of reversible protein interactions with small molecule compounds. The manually curated binding data are linked to protein-ligand crystal structures, enabling structure-thermodynamics correlations to be determined. The database contains over 5500 binding datasets of 556 sulfonamide compound interactions with the 12 catalytically active human carbonic anhydrase isozymes defined by fluorescent thermal shift assay, isothermal titration calorimetry, inhibition of enzymatic activity and surface plasmon resonance. In the PLBD, the intrinsic thermodynamic parameters of interactions are provided, which account for the binding-linked protonation reactions. In addition to the protein-ligand binding affinities, the database provides calorimetrically measured binding enthalpies, providing additional mechanistic understanding. The PLBD can be applied to investigations of protein-ligand recognition and could be integrated into small molecule drug design. Database URL https://plbd.org/
AB - We introduce a protein-ligand binding database (PLBD) that presents thermodynamic and kinetic data of reversible protein interactions with small molecule compounds. The manually curated binding data are linked to protein-ligand crystal structures, enabling structure-thermodynamics correlations to be determined. The database contains over 5500 binding datasets of 556 sulfonamide compound interactions with the 12 catalytically active human carbonic anhydrase isozymes defined by fluorescent thermal shift assay, isothermal titration calorimetry, inhibition of enzymatic activity and surface plasmon resonance. In the PLBD, the intrinsic thermodynamic parameters of interactions are provided, which account for the binding-linked protonation reactions. In addition to the protein-ligand binding affinities, the database provides calorimetrically measured binding enthalpies, providing additional mechanistic understanding. The PLBD can be applied to investigations of protein-ligand recognition and could be integrated into small molecule drug design. Database URL https://plbd.org/
UR - http://www.scopus.com/inward/record.url?scp=85163906607&partnerID=8YFLogxK
U2 - 10.1093/database/baad040
DO - 10.1093/database/baad040
M3 - 期刊論文
C2 - 37290059
AN - SCOPUS:85163906607
SN - 1758-0463
VL - 2023
JO - Database : the journal of biological databases and curation
JF - Database : the journal of biological databases and curation
M1 - baad040
ER -