Homology modeling of Mycoplasma pneumoniae enolase and its molecular interaction with human plasminogen.

ABSTRACT: Alpha (alpha)-enolase (e), a glycolytic enzyme, has an alternative role as a surface receptor of several bacteria mediating plasminogen (pg) binding. It is also recognized as a virulence factor of some pathogenic bacteria facilitating plasminogen activation and host cell invasion. A mycoplasmal alpha-enolase is also a plasminogen binding protein. Molecular interactions of enolase from Mycoplasma pneumoniae with host plasminogen would be useful for exploring the pathogen-host interaction. In an attempt to identify plasminogen binding sites of M. pneumoniae enolase, homology modeling and docking studies were conducted to obtain modeled structures of the M. pneumoniae enolase-plasminogen complex. The refined model was validated further by standard methods. Molecular docking revealed hydrogen

SUBMITTER: Chumchua V 

PROVIDER: S-EPMC2586135 | biostudies-literature | 2008

REPOSITORIES: biostudies-literature