Structural and functional aspects of snake venoms metalloproteinases (SVMPs) have been extensively studied due to their role in envenomation. However, in the detection of certain coagulation disorders these biomolecules have been used and applied for the production of new thrombolytic drugs. CcMP-II, a SVMP-II metalloproteinase with a hemorrhagic activity, isolated from the venom of Cerastes cerastes, its sequence of 472 amino acids was identified. Predicted 3D structure showed an arrangement of CcMP-II into two distinct domains: i) a metalloproteinase domain where the zinc-binding motif is found (HXXGHNLGIDH) in addition to the sequence Cys‐Ile‐Met (CIM) at the Met-turn and ii) disintegrin-like domain containing RGD motif. CcMP-II inhibits platelet aggregation induced by collagen in a dose-dependent manner with an IC₅₀ value estimated of 0.11 nM. This proteinase inhibits also aggregation of platelet stimulated by collagen even if the metal chelating agents (EDTA and 1, 10-phenontroline) are present suggesting that anti-aggregating effect is not due to its metalloproteinase domain, but to its disintegrin-like domain. Capillary pathological modifications caused by CcMP-II following intramuscular injection have as well been examined in mice. The key morphological alterations of the capillary vessels were clearly apparent from the ultrastructural study. The CcMP-II can play a key function in the pathogenesis of disorders that occurs following envenomation of Cerastes cerastes. The three-dimensional model of CcMP-II was built to explain structure–function relationships in ADAM/ADAMTs, a family of proteins having significant therapeutic potential. In order to explain structure–function relationships in ADAM / ADAMT, a family of proteins with considerable therapeutic potential, the three-dimensional model of CcMP-II was constructed.

蛇毒金属蛋白酶 (SVMP) 的结构和功能方面因其在毒液中的作用而得到广泛研究。然而，在检测某些凝血障碍时，这些生物分子已被用于生产新的溶栓药物。CCMP-II，一个SVMP-II金属蛋白酶与出血的活性，从毒液中分离角蝰，其 472 个氨基酸的序列被确定。预测的 3D 结构显示 CcMP-II 排列成两个不同的结构域：i) 除了在 Met 转角处的序列 Cys-Ile-Met (CIM) 之外，还发现了锌结合基序的金属蛋白酶结构域 (HXXGHNLGIDH) 和ii) 含有 RGD 基序的去整合素样结构域。CcMP-II 以剂量依赖的方式抑制胶原诱导的血小板聚集，IC ₅₀估计值为 0.11 nM。即使存在金属螯合剂（EDTA 和 1, 10-phenontroline），这种蛋白酶也能抑制由胶原蛋白刺激的血小板聚集，这表明抗聚集作用不是由于其金属蛋白酶结构域，而是由于其解聚素样结构域。肌肉注射后由 CcMP-II 引起的毛细血管病理改变也在小鼠中进行了检查。从超微结构研究中可以清楚地看出毛细血管的关键形态学改变。该CCMP-II可以在疾病的发病中起了关键作用发生以下咬伤角蝰. CcMP-II 的三维模型旨在解释 ADAM/ADAMTs 中的结构-功能关系，ADAM/ADAMTs 是一个具有显着治疗潜力的蛋白质家族。为了解释具有相当治疗潜力的蛋白质家族ADAM/ADAMT中的结构-功能关系，构建了CcMP-II的三维模型。