The protease enzyme, matrix metalloproteinase-2 (MMP-2) has been a target of choice for the drug development due to its multi-façade involvement in numerous diseased conditions including cancer. To find a selective MMP-2 inhibitor several computational strategies are employed in its design and discovery. In these strategies, protein structure of MMP-2 is an inevitable part to formulate effective structure-based drug design (SBDD) of selective MMP-2 inhibitors. In the present communication, several crystal structures of MMP-2 have been analyzed with different statistical parameters and their implementations in SBDD of inhibitors are scrutinized. In addition, binding mode analyses of various classes of inhibitors are discussed to pinpoint the effective design of selective inhibitors by maximizing its interaction with the MMP-2 enzyme binding site. This may provide a crucial insight for exploring the numerous possibilities for SBDD of MMP-2 inhibitors to accelerate anticancer drug discovery efforts.

蛋白酶、基质金属蛋白酶-2 (MMP-2) 一直是药物开发的目标选择，因为它在多种疾病（包括癌症）中具有多面性。为了找到选择性 MMP-2 抑制剂，在其设计和发现中采用了几种计算策略。在这些策略中，MMP-2 的蛋白质结构是制定有效的选择性 MMP-2 抑制剂基于结构的药物设计 (SBDD) 的必然部分。在本通讯中，已经使用不同的统计参数分析了 MMP-2 的几种晶体结构，并仔细检查了它们在 SBDD 抑制剂中的实施。此外，讨论了各类抑制剂的结合模式分析，以通过最大化其与 MMP-2 酶结合位点的相互作用来确定选择性抑制剂的有效设计。