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 t

SUBMITTER: Zhao Y 

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

REPOSITORIES: biostudies-literature