三硫键胰蛋白酶抑制剂EETI II折叠过程中稳定的[9-21, 15-27] 2二硫键中间体的表征及二维核磁共振研究
Characterization and 2D NMR study of the stable [9-21, 15-27] 2 disulfide intermediate in the folding of the 3 disulfide trypsin inhibitor EETI II.
作者信息
Le-Nguyen D, Heitz A, Chiche L, el Hajji M, Castro B
机构信息
CCIPE, Montpellier, France.
出版信息
Protein Sci. 1993 Feb;2(2):165-74. doi: 10.1002/pro.5560020205.
Abstract
The three disulfide Ecballium elaterium trypsin inhibitor II (EETI II) reduction with dithiothreitol (DTT) and reoxidation of the fully reduced derivative have been examined. A common stable intermediate has been observed for both processes. Isolation and sequencing of carboxymethylated material showed that the intermediate lacks the [2-19] bridge. The NMR study showed a very strong structural conservation as compared to the native EETI II, suggesting that the bridges are the [9-21] and [15-27] native ones. The differences occurred in sections 2-7 (containing the free cysteine 2 and the Arg 4-Ile 5 active site) and 19-21 (containing the second free cysteine). Distance geometry calculations and restrained molecular dynamics refinements were also in favor of a [9-21, 15-27] arrangement and resulted in a well-conserved (7-28) segment.
摘要
用二硫苏糖醇（DTT）对三种二硫键的喷瓜胰蛋白酶抑制剂II（EETI II）进行还原，并对完全还原的衍生物进行再氧化，已对其进行了研究。在这两个过程中均观察到一种常见的稳定中间体。羧甲基化物质的分离和测序表明，该中间体缺乏[2-19]桥。核磁共振研究表明，与天然EETI II相比，其结构具有很强的保守性，这表明这些桥是天然的[9-21]和[15-27]桥。差异出现在第2-7节（包含游离半胱氨酸2和Arg 4-Ile 5活性位点）和第19-21节（包含第二个游离半胱氨酸）。距离几何计算和受限分子动力学优化也支持[9-21, 15-27]的排列，并产生了一个保守性良好的（7-28）片段。
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本文引用的文献
1
Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution.
J Mol Biol. 1982 Sep 25;160(3):475-98. doi: 10.1016/0022-2836(82)90309-6.
2
The 'knotting' problem in proteins. Loop penetration.
Biochim Biophys Acta. 1980 Nov 20;626(1):97-105. doi: 10.1016/0005-2795(80)90201-9.
3
Isolation and partial amino acid sequence of the trypsin inhibitor from the seeds of Cucurbita maxima.笋瓜种子胰蛋白酶抑制剂的分离及部分氨基酸序列分析
Acta Biochim Pol. 1980;27(3-4):371-82.
4
Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance.用于通过核磁共振测量分子内质子-质子距离约束来研究蛋白质构象的20种常见氨基酸的伪结构。
J Mol Biol. 1983 Oct 5;169(4):949-61. doi: 10.1016/s0022-2836(83)80144-2.
5
Structure of the toxic domain of the Escherichia coli heat-stable enterotoxin ST I.大肠杆菌热稳定肠毒素ST I毒性结构域的结构
Biochemistry. 1986 Dec 2;25(24):7854-66. doi: 10.1021/bi00372a011.
6
Synthesis and secondary-structure determination of omega-conotoxin GVIA: a 27-peptide with three intramolecular disulfide bonds.
Biopolymers. 1986;25 Suppl:S61-8.
7
The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes.
FEBS Lett. 1989 Jan 2;242(2):285-92. doi: 10.1016/0014-5793(89)80486-7.
8
1H 2D NMR and distance geometry study of the folding of Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family.南瓜抑制剂家族成员——喷瓜胰蛋白酶抑制剂折叠的1H 2D NMR及距离几何学研究
Biochemistry. 1989 Mar 21;28(6):2392-8. doi: 10.1021/bi00432a009.
9
Protease inhibitors from Ecballium elaterium seeds.
Int J Pept Protein Res. 1989 Mar;33(3):202-8. doi: 10.1111/j.1399-3011.1989.tb00210.x.
10
Solid phase synthesis of a trypsin inhibitor isolated from the Cucurbitaceae Ecballium elaterium.
Int J Pept Protein Res. 1989 Dec;34(6):492-7. doi: 10.1111/j.1399-3011.1989.tb01399.x.
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