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首页> 外文期刊>Journal of Molecular Biology >SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE
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SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE

机译：R-ELAFIN的溶液结构，一种弹性蛋白酶的特异性抑制剂

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The solution structure of r-elafin, a specific elastase inhibitor, has been determined using NMR spectroscopy. Characterized by a flat core and a flexible N-terminal extremity, the three-dimensional structure is formed by a central twisted beta-hairpin accompanied by two external segments linked by the proteinase binding loop. A cluster of three disulfide bridges connects the external segments to the central beta-sheet and a single fourth disulfide bridge links the binding loop to the central beta-turn. The same spatial distribution of disulfide bridges can be observed in both domains of the secretory leukocyte protease inhibitor (SLPI), another elastase inhibitor. The structural homology between r-elafin and the C-terminal domain of SLPI confirms the former as a second member of the chelonianin family of proteinase inhibitors. Based on the homology between the two proteins and recent results obtained for elastase binding mutants of the bovine pancreatic trypsin inhibitor (BPTI), we define the segment 22 to 27 as the binding loop of elafin, with the scissile peptide bond between Ala24 and Met25. In our solution structures, this loop is extended and solvent-exposed, and exhibits a large degree of flexibility. This mobility, already observed for the binding loop in other protease inhibitors in solution, might be an important feature for the interaction with the corresponding protease. (C) 1997 Academic Press Limited. [References: 47]
机译：r-elafin（一种特定的弹性蛋白酶抑制剂）的溶液结构已使用NMR光谱法确定。具有扁平核和灵活的N末端末端的特征，三维结构由中央扭曲的β-发夹形结构形成，并伴有两个通过蛋白酶结合环连接的外部区段。三个三硫键桥的簇将外部片段连接到中央β-折叠，单个第四硫键将连接环连接到中央β-转角。可以在另一种弹性蛋白酶抑制剂分泌型白细胞蛋白酶抑制剂（SLPI）的两个域中观察到二硫键的空间分布相同。 r-elafin和SLPI的C末端结构域之间的结构同源性证实前者是蛋白酶抑制剂chelonianin家族的第二个成员。基于这两种蛋白质之间的同源性以及牛胰胰蛋白酶抑制剂（BPTI）的弹性蛋白酶结合突变体获得的最新结果，我们将22至27段定义为弹性蛋白的结合环，在Ala24和Met25之间具有易断裂的肽键。在我们的解决方案结构中，此回路经过扩展和溶剂暴露，并表现出很大的灵活性。对于溶液中其他蛋白酶抑制剂中的结合环已经观察到的这种迁移性可能是与相应蛋白酶相互作用的重要特征。 （C）1997 Academic Press Limited。 [参考：47]

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