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动力学和热力学研究表明，具有几乎相同三级结构的趋化因子同系物CC11和CC24具有不同的折叠途径。

Kinetic and thermodynamic studies reveal chemokine homologues CC11 and CC24 with an almost identical tertiary structure have different folding pathways.

作者信息

Ge Baosheng, Jiang Xiaoyong, Chen Yao, Sun Tingting, Yang Qiuxia, Huang Fang

机构信息

Center for Bioengineering and Biotechnology, China University of Petroleum (East China), Qingdao, 266580 People's Republic of China.

出版信息

BMC Biophys. 2017 Sep 12;10:7. doi: 10.1186/s13628-017-0039-4. eCollection 2017.

DOI:10.1186/s13628-017-0039-4
PMID:28919974
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5596964/
Abstract

BACKGROUND

Proteins with low sequence identity but almost identical tertiary structure and function have been valuable to uncover the relationship between sequence, tertiary structure, folding mechanism and functions. Two homologous chemokines, CCL11 and CCL24, with low sequence identity but similar tertiary structure and function, provide an excellent model system for respective studies.

RESULTS

The kinetics and thermodynamics of the two homologous chemokines were systematically characterized. Despite their similar tertiary structures, CCL11 and CCL24 show different thermodynamic stability in guanidine hydrochloride titration, with D = 2.20 M and 4.96 M, respectively. The kinetics curves clearly show two phases in the folding/unfolding processes of both CCL11 and CCL24, which suggests the existence of an intermediate state in their folding/unfolding processes. The folding pathway of both CCL11 and CCL24 could be well described using a folding model with an on-pathway folding intermediate. However, the folding kinetics and stability of the intermediate state of CCL11 and CCL24 are obviously different.

CONCLUSION

Our results suggest homologous proteins with low sequence identity can display almost identical tertiary structure, but very different folding mechanisms, which applies to homologues in the chemokine protein family, extending the general applicability of the above observation.

摘要

背景

具有低序列同一性但几乎相同的三级结构和功能的蛋白质对于揭示序列、三级结构、折叠机制和功能之间的关系具有重要价值。两种同源趋化因子CCL11和CCL24，具有低序列同一性但相似的三级结构和功能，为各自的研究提供了一个出色的模型系统。

结果

系统地表征了这两种同源趋化因子的动力学和热力学性质。尽管它们具有相似的三级结构，但CCL11和CCL24在盐酸胍滴定中表现出不同的热力学稳定性，其变性剂浓度分别为2.20 M和4.96 M。动力学曲线清楚地显示了CCL11和CCL24折叠/去折叠过程中的两个阶段，这表明它们的折叠/去折叠过程中存在一个中间状态。CCL11和CCL24的折叠途径都可以用一个具有折叠中间态的折叠模型很好地描述。然而，CCL11和CCL24中间态的折叠动力学和稳定性明显不同。

结论

我们的结果表明，具有低序列同一性的同源蛋白质可以显示几乎相同的三级结构，但折叠机制非常不同，这适用于趋化因子蛋白家族中的同源物，扩展了上述观察结果的普遍适用性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/94e91f5ae138/13628_2017_39_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/016e7ffbdda1/13628_2017_39_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/c66a67d1e07c/13628_2017_39_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/44579a2cd49e/13628_2017_39_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/84b4028934bb/13628_2017_39_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/8204d45cc3ba/13628_2017_39_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/94e91f5ae138/13628_2017_39_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/016e7ffbdda1/13628_2017_39_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/c66a67d1e07c/13628_2017_39_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/44579a2cd49e/13628_2017_39_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/84b4028934bb/13628_2017_39_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/8204d45cc3ba/13628_2017_39_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d50/5596964/94e91f5ae138/13628_2017_39_Fig6_HTML.jpg

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