PLBD

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.本研究介绍了一款蛋白质-配体结合数据库（protein-ligand binding database, PLBD），该库收录了小分子化合物与蛋白质发生可逆相互作用的热力学与动力学数据。经人工整理校验的结合数据与蛋白质-配体晶体结构相关联，可用于解析结构-热力学相关性。该数据库包含556种磺酰胺类化合物与12种具有催化活性的人类碳酸酐酶同工酶的共5500余条结合数据集，相关数据通过荧光热漂移实验、等温滴定量热法、酶活性抑制实验以及表面等离子体共振实验确定。PLBD中收录了相互作用的固有热力学参数，这些参数涵盖了与结合过程相关联的质子化反应。除蛋白质-配体结合亲和力外，该数据库还提供了量热法测得的结合焓，可助力进一步解析相互作用的分子机制。PLBD可应用于蛋白质-配体识别相关研究，也可集成应用于小分子药物设计工作。

搜集汇总

背景与挑战

背景概述

PLBD是一个专注于蛋白质与小分子配体相互作用的数据库，提供内在的热力学和动力学参数，包括结合亲和力和焓变数据，并关联X射线晶体结构。该数据库主要涵盖人类碳酸酐酶和热休克蛋白等蛋白质，旨在支持蛋白质-配体识别研究和药物设计。