Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins
| Autor: | Zhichao Liu, Yunjie Zhao, Zhangyong Li, Chen Zeng, Hang Liu, Qin Liu, Chanyou Chen, Yiren Jian, H. Howie Huang, Lu Wang |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation Sequence analysis Dimer Science Complex formation Article Structure-Activity Relationship 03 medical and health sciences chemistry.chemical_compound Potential mechanism Binding Sites Multidisciplinary biology Mechanism (biology) Lectin Bulb 030104 developmental biology Biochemistry chemistry biology.protein Medicine Plant Lectins Protein Multimerization Mannose Linker Algorithms Protein Binding |
| Zdroj: | Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017) Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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