当前位置: X-MOL 学术Acta Cryst. F › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.
Acta Crystallographica Section F ( IF 1.072 ) Pub Date : 2019-06-17 , DOI: 10.1107/s2053230x19006046
Shaunivan L Labiuk 1 , Jurgen Sygusch 2 , Pawel Grochulski 1
Affiliation  

Neutral endopeptidase (neprilysin; NEP) is a proteinase that cleaves a wide variety of peptides and has been implicated in Alzheimer's disease, cardiovascular conditions, arthritis and other inflammatory diseases. The structure of the soluble extracellular domain (residues 55–750) of rabbit neprilysin was solved both in its native form at 2.1 Å resolution, and bound to the inhibitors phosphoramidon and thiorphan at 2.8 and 3.0 Å resolution, respectively. Consistent with the extracellular domain of human neprilysin, the structure reveals a large central cavity which contains the active site and the location for inhibitor binding.

中文翻译:

可溶性兔中性溶血素与磷酰胺或硫醇复合的结构。

中性内肽酶(neprilysin; NEP)是一种可裂解多种肽的蛋白酶,与阿尔茨海默氏病,心血管疾病,关节炎和其他炎症性疾病有关。兔脑啡肽酶的可溶性细胞外结构域(残基55-750)的结构以其天然形式以2.1Å的分辨率被解析,并分别以2.8和3.0Å的分辨率与抑制剂磷酰胺和噻吩结合。与人脑啡肽酶的胞外域一致,该结构揭示了一个大的中心腔,该中心腔包含活性位点和抑制剂结合的位置。
更新日期:2019-06-17
down
wechat
bug