Suppr超能文献

单个氨基酸可改变软骨基质蛋白α-螺旋卷曲螺旋结构域的寡聚化状态。

A single amino acid can switch the oligomerization state of the alpha-helical coiled-coil domain of cartilage matrix protein.

作者信息

Beck K, Gambee J E, Kamawal A, Bächinger H P

机构信息

Shriners Hospital for Children, Research Unit, Portland, OR 97201, USA.

出版信息

EMBO J. 1997 Jul 1;16(13):3767-77. doi: 10.1093/emboj/16.13.3767.

Abstract

We have studied the oligomerization of an alpha-helical coiled-coil using as an example a peptide corresponding to the C-terminal domain of cartilage matrix protein. By replacing one arginine residue, which forms an interchain ionic interaction with a glutamic acid residue, with glutamine, we found that this peptide assembles into a homotetramer at neutral pH in contrast to the native molecule which forms homotrimers. At acidic and basic pH, however, we again observed the trimer conformation. Another arginine, which is probably involved in an intrachain salt bridge, has no effect on the assembly. Our data demonstrate that besides the specific distribution of hydrophobic residues, interchain ionic interactions can be crucial in modulating the association behavior of alpha-helical coiled-coil domains.

摘要

我们以对应于软骨基质蛋白C末端结构域的肽为例,研究了α-螺旋卷曲螺旋的寡聚化。通过用谷氨酰胺取代一个与谷氨酸残基形成链间离子相互作用的精氨酸残基,我们发现该肽在中性pH下组装成同四聚体,这与形成同三聚体的天然分子不同。然而,在酸性和碱性pH下,我们再次观察到三聚体构象。另一个可能参与链内盐桥形成的精氨酸对组装没有影响。我们的数据表明,除了疏水残基的特定分布外,链间离子相互作用在调节α-螺旋卷曲螺旋结构域的缔合行为中可能至关重要。

相似文献

引用本文的文献

2
Protein Design: From the Aspect of Water Solubility and Stability.蛋白质设计:从水溶性和稳定性方面考虑。
Chem Rev. 2022 Sep 28;122(18):14085-14179. doi: 10.1021/acs.chemrev.1c00757. Epub 2022 Aug 3.
10
A conserved trimerization motif controls the topology of short coiled coils.一个保守的三聚化基序控制着短卷曲螺旋的拓扑结构。
Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13891-6. doi: 10.1073/pnas.0502390102. Epub 2005 Sep 19.

本文引用的文献

8
Predicting oligomerization states of coiled coils.预测卷曲螺旋的寡聚化状态。
Protein Sci. 1995 Aug;4(8):1596-607. doi: 10.1002/pro.5560040818.

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验