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晶体中的一种设计合成的β-发夹肽。

A designed beta-hairpin peptide in crystals.

作者信息

Karle I L, Awasthi S K, Balaram P

机构信息

Laboratory for the Structure of Matter, Naval Research Laboratory, Washington, DC 20375-5341, USA.

出版信息

Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8189-93. doi: 10.1073/pnas.93.16.8189.

Abstract

Beta-hairpin structures have been crystallographically characterized only in very short acyclic peptides, in contrast to helices. The structure of the designed beta-hairpin, t-butoxycarbonyl-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe in crystals is described. The two independent molecules of the octapeptide fold into almost ideal beta-hairpin conformations with the central D-Pro-Gly segment adopting a Type II' beta-turn conformation. The definitive characterization of a beta-hairpin has implications for de novo peptide and protein design, particularly for the development of three- and four-stranded beta-sheets.

摘要

与螺旋结构不同,β-发夹结构仅在非常短的无环肽中通过晶体学进行了表征。本文描述了设计的β-发夹结构——叔丁氧羰基-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe在晶体中的结构。八肽的两个独立分子折叠成几乎理想的β-发夹构象,中心的D-Pro-Gly片段采用II'型β-转角构象。β-发夹结构的确切表征对从头肽和蛋白质设计具有重要意义,特别是对于三链和四链β-折叠片层的开发。

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A designed beta-hairpin peptide in crystals.晶体中的一种设计合成的β-发夹肽。
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本文引用的文献

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Structure of octreotide, a somatostatin analogue.奥曲肽(一种生长抑素类似物)的结构。
Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):48-59. doi: 10.1107/S0907444994006104.
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Crystal structures of peptides and modified peptides.
Biopolymers. 1996;40(1):45-83. doi: 10.1002/(sici)1097-0282(1996)40:1<45::aid-bip3>3.0.co;2-3.
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De novo design of beta-sheet proteins.β-折叠蛋白质的从头设计。
Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):8729-30. doi: 10.1073/pnas.91.19.8729.

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