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模拟非洲爪蟾皮肤内蛋白酶识别的RXVRG共有序列的十四肽的结构测定:一种基于模拟退火和一维核磁共振的方法

Structure determination of a tetradecapeptide mimicking the RXVRG consensus sequence recognized by a Xenopus laevis skin endoprotease: an approach based on simulated annealing and 1H NMR.

作者信息

Meddeb S, Chalaoux F R, Ballini J P, Baron D, Vigny P, Demaret J P

机构信息

L.P.C.B., Institut Curie et Université Paris VI, France.

出版信息

J Comput Aided Mol Des. 1995 Apr;9(2):160-70. doi: 10.1007/BF00124406.

DOI:10.1007/BF00124406
PMID:7608747
Abstract

The tetradecapeptide of sequence H-Asp-Val-Asp-Glu-Arg5-Asp-Val-Arg-Gly9-Phe-Ala-Ser-Phe-Leu- NH2 is recognized by a putative maturation endoprotease of the Xenopus laevis skin, which cleaves between Arg8 and Gly9. A conformational search has been performed on this peptide by simulated annealing calculations. Two different models in agreement with the NMR data were found. The conformational difference between the two types of model is located in the consensus sequence, i.e., from Arg5 to Gly9.

摘要

序列为H-Asp-Val-Asp-Glu-Arg5-Asp-Val-Arg-Gly9-Phe-Ala-Ser-Phe-Leu-NH2的十四肽可被非洲爪蟾皮肤中一种假定的成熟内切蛋白酶识别,该酶在Arg8和Gly9之间切割。通过模拟退火计算对该肽进行了构象搜索。发现了两种与核磁共振数据一致的不同模型。两种模型类型之间的构象差异位于共有序列中,即从Arg5到Gly9。

相似文献

1
Structure determination of a tetradecapeptide mimicking the RXVRG consensus sequence recognized by a Xenopus laevis skin endoprotease: an approach based on simulated annealing and 1H NMR.模拟非洲爪蟾皮肤内蛋白酶识别的RXVRG共有序列的十四肽的结构测定:一种基于模拟退火和一维核磁共振的方法
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2
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Conformational studies of an undecapeptide reproducing the consensus sequence around the cleavage site of the RXVRG endoprotease from Xenopus laevis skin.对一种十一肽的构象研究,该十一肽再现了非洲爪蟾皮肤中RXVRG内切蛋白酶切割位点周围的共有序列。
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本文引用的文献

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