Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins

Abstract The bulb-type lectins are proteins consist of three sequential beta-sheet subdomains that bind to specific carbohydrates to perform certain biological functions. The active states of most bulb-type lectins are dimeric and it is thus important to elucidate the short- and long-range recogniti...

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Autores principales:	Yunjie Zhao, Yiren Jian, Zhichao Liu, Hang Liu, Qin Liu, Chanyou Chen, Zhangyong Li, Lu Wang, H. Howie Huang, Chen Zeng
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/304dcbb78a7a4df48d8b3f279fdca04a
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spelling	oai:doaj.org-article:304dcbb78a7a4df48d8b3f279fdca04a2021-12-02T16:06:47ZNetwork Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins10.1038/s41598-017-03003-52045-2322https://doaj.org/article/304dcbb78a7a4df48d8b3f279fdca04a2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03003-5https://doaj.org/toc/2045-2322Abstract The bulb-type lectins are proteins consist of three sequential beta-sheet subdomains that bind to specific carbohydrates to perform certain biological functions. The active states of most bulb-type lectins are dimeric and it is thus important to elucidate the short- and long-range recognition mechanism for this dimer formation. To do so, we perform comparative sequence analysis for the single- and double-domain bulb-type lectins abundant in plant genomes. In contrast to the dimer complex of two single-domain lectins formed via protein-protein interactions, the double-domain lectin fuses two single-domain proteins into one protein with a short linker and requires only short-range interactions because its two single domains are always in close proximity. Sequence analysis demonstrates that the highly variable but coevolving polar residues at the interface of dimeric bulb-type lectins are largely absent in the double-domain bulb-type lectins. Moreover, network analysis on bulb-type lectin proteins show that these same polar residues have high closeness scores and thus serve as hubs with strong connections to all other residues. Taken together, we propose a potential mechanism for this lectin complex formation where coevolving polar residues of high closeness are responsible for long-range recognition.Yunjie ZhaoYiren JianZhichao LiuHang LiuQin LiuChanyou ChenZhangyong LiLu WangH. Howie HuangChen ZengNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yunjie Zhao Yiren Jian Zhichao Liu Hang Liu Qin Liu Chanyou Chen Zhangyong Li Lu Wang H. Howie Huang Chen Zeng Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins
description	Abstract The bulb-type lectins are proteins consist of three sequential beta-sheet subdomains that bind to specific carbohydrates to perform certain biological functions. The active states of most bulb-type lectins are dimeric and it is thus important to elucidate the short- and long-range recognition mechanism for this dimer formation. To do so, we perform comparative sequence analysis for the single- and double-domain bulb-type lectins abundant in plant genomes. In contrast to the dimer complex of two single-domain lectins formed via protein-protein interactions, the double-domain lectin fuses two single-domain proteins into one protein with a short linker and requires only short-range interactions because its two single domains are always in close proximity. Sequence analysis demonstrates that the highly variable but coevolving polar residues at the interface of dimeric bulb-type lectins are largely absent in the double-domain bulb-type lectins. Moreover, network analysis on bulb-type lectin proteins show that these same polar residues have high closeness scores and thus serve as hubs with strong connections to all other residues. Taken together, we propose a potential mechanism for this lectin complex formation where coevolving polar residues of high closeness are responsible for long-range recognition.
format	article
author	Yunjie Zhao Yiren Jian Zhichao Liu Hang Liu Qin Liu Chanyou Chen Zhangyong Li Lu Wang H. Howie Huang Chen Zeng
author_facet	Yunjie Zhao Yiren Jian Zhichao Liu Hang Liu Qin Liu Chanyou Chen Zhangyong Li Lu Wang H. Howie Huang Chen Zeng
author_sort	Yunjie Zhao
title	Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins
title_short	Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins
title_full	Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins
title_fullStr	Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins
title_full_unstemmed	Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins
title_sort	network analysis reveals the recognition mechanism for dimer formation of bulb-type lectins
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/304dcbb78a7a4df48d8b3f279fdca04a
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_version_	1718384833451786240

Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins

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