THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN
THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN
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DOI：
10.1111/j.1432-1033.1987.tb13600.x
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发表时间：
1987-11-16
期刊：
影响因子：
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通讯作者：
SZELKE, M
中科院分区：
文献类型：
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作者：
COOPER, J;FOUNDLING, S;SZELKE, M
已通过X射线衍射在0.20 nm分辨率下测定了与真菌天冬氨酸蛋白酶内皮硫肽酶（EC 3.4.23.6）活性位点结合的合成多肽抑制剂的构象，并将其精确至0.20的一致因子。抑制剂： 基于胃蛋白酶的显色底物（EC 3.4.23.1）。取代易裂键的是一个还原的肽基团，该基团抗水解并模拟四面体过渡态。抑制剂以延伸构象结合，还原键靠近酶的必需天冬氨酸侧链。酶和抑制剂之间的氢键和疏水相互作用不会引起大的构象变化。
The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been determined by X‐ray diffraction at 0.20‐nm resolution and refined to an agreement factor of 0.20. The inhibitor: is based on a chromogenic substrate of pepsin (EC 3.4.23.1). It has, in place of the scissile bond, a reduced peptide group which is resistant to hydrolysis and mimics the tetrahedral transition state. The inhibitor binds in an extended conformation with the reduced bond close to the essential aspartate side‐chains of the enzyme. The hydrogen bonds and hydrophobic interactions between the enzyme and the inhibitor do not induce large conformational changes.