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首页> 外文期刊>FEBS Open Bio >A new high-resolution crystal structure of the Drosophila melanogaster angiotensin converting enzyme homologue, AnCE
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A new high-resolution crystal structure of the Drosophila melanogaster angiotensin converting enzyme homologue, AnCE

机译：果蝇血管紧张素转化酶同系物AnCE的新型高分辨率晶体结构

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Angiotensin converting enzyme (ACE) is a zinc-dependent dipeptidyl carboxypeptidase with an essential role in blood pressure homeostasis in mammals. ACE has long been targeted in the treatment of hypertension through ACE inhibitors, however current inhibitors are known to cause severe side effects. Therefore, there is a requirement for a new generation of ACE inhibitors and structural information will be invaluable in their development. ACE is a challenging enzyme to work with due to its extensive glycosylation. As such, the Drosophila melanogaster ACE homologue, AnCE, which shares ~60% sequence similarity with human ACE, can be used as a model for studying inhibitor binding. The presence of ligands originating from the crystallisation condition at the AnCE active site has proved an obstacle to studying the binding of new inhibitor precursors. Here we present the crystal structure of AnCE (in a new crystal form) at 1.85A resolution, using crystals grown under different conditions. This new structure may be more suitable for studying the binding of new compounds, with the potential of developing a new generation of improved ACE inhibitors.
机译：血管紧张素转换酶（ACE）是锌依赖性的二肽基羧肽酶，在哺乳动物的血压稳态中起着重要的作用。长期以来，ACE一直是通过ACE抑制剂治疗高血压的目标，但已知目前的抑制剂会引起严重的副作用。因此，需要新一代的ACE抑制剂，并且结构信息在其开发中将是无价的。由于其广泛的糖基化作用，ACE是一种具有挑战性的酶。因此，果蝇果蝇ACE同源物AnCE与人ACE具有约60％的序列相似性，可以用作研究抑制剂结合的模型。已证明在AnCE活性位点存在源自结晶条件的配体，这已成为研究新抑制剂前体结合的障碍。在这里，我们使用在不同条件下生长的晶体，以1.85A的分辨率呈现AnCE的晶体结构（以新的晶体形式）。这种新结构可能更适合研究新化合物的结合，并具有开发新一代改良ACE抑制剂的潜力。

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