Abstract Molecular docking of a 3D model of bovine testicular hyaluronidase was performed with dimers and trimers of chondroitin. On the molecular surface of a hyaluronidase globule, eight sites for ligand binding were established. Sites 6, 3, and 1 of the enzyme structure were found to be the most important sites since chondroitin binding therewith distorts the protein 3D structure. The interactions of enzyme structure with chondroitin ligands are mainly determined by electrostatic forces. For free hyaluronidase molecule (without ligands) at temperatures above 300 K conformational transfers leading to the enzyme inactivation were noted. The inactivation was mainly manifested through irreversible attraction of the protein fragment surrounding the Glu-105 residue and the one between Arg-59 and Arg-96, where a temperature decrease did not induce the restoration of the initial view of 3D structure of the enzyme molecule. Binding of chondroitin ligands to the enzyme structure at positions 6, 3, and 1 increased its denaturation temperature by approximately 10 degrees. The most significant effect of enzyme structure stabilization was provided by chondroitin ligand binding with hyaluronidase at site 6. This effect of protein structure stabilization exceeded the one of chondroitin sulfate trimers against the enzyme inhibition by heparin tetramers, which required binding of four to five chondroitin sulfate ligands on the molecular surface of the enzyme.

中文翻译：

---

牛睾丸透明质酸酶分子对接中软骨素二聚体和三聚体的研究

摘要 牛睾丸透明质酸酶的 3D 模型与软骨素的二聚体和三聚体进行了分子对接。在透明质酸酶小球的分子表面上，建立了八个配体结合位点。发现酶结构的位点 6、3 和 1 是最重要的位点，因为与其结合的软骨素会扭曲蛋白质 3D 结构。酶结构与软骨素配体的相互作用主要由静电力决定。对于在高于 300 K 的温度下的游离透明质酸酶分子（无配体），注意到导致酶失活的构象转移。失活主要通过围绕 Glu-105 残基和 Arg-59 和 Arg-96 残基之间的蛋白质片段的不可逆吸引表现出来，其中温度降低不会诱导酶分子 3D 结构的初始视图的恢复。软骨素配体与位置 6、3 和 1 的酶结构的结合使其变性温度增加了大约 10 度。酶结构稳定的最显着影响是软骨素配体与透明质酸酶在位点 6 结合。这种蛋白质结构稳定的作用超过了硫酸软骨素三聚体之一对肝素四聚体的酶抑制作用，肝素四聚体需要结合四到五个硫酸软骨素酶分子表面的配体。和 1 将其变性温度提高了大约 10 度。酶结构稳定的最显着影响是软骨素配体与透明质酸酶在位点 6 结合。这种蛋白质结构稳定的作用超过了硫酸软骨素三聚体之一对肝素四聚体的酶抑制作用，肝素四聚体需要结合四到五个硫酸软骨素酶分子表面的配体。和 1 将其变性温度提高了大约 10 度。酶结构稳定的最显着影响是软骨素配体与透明质酸酶在位点 6 结合。这种蛋白质结构稳定的作用超过了硫酸软骨素三聚体之一对肝素四聚体的酶抑制作用，肝素四聚体需要结合四到五个硫酸软骨素酶分子表面的配体。