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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 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.

SUBMITTER: Zhao Y 

PROVIDER: S-EPMC5460271 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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

Zhao Yunjie Y   Jian Yiren Y   Liu Zhichao Z   Liu Hang H   Liu Qin Q   Chen Chanyou C   Li Zhangyong Z   Wang Lu L   Huang H Howie HH   Zeng Chen C  

Scientific reports 20170606 1


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  ...[more]

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