Characterizing structural features of cuticle-degrading proteases from fungi by molecular modeling.

ABSTRACT:

Background

Serine proteases secreted by nematode and insect pathogenic fungi are bio-control agents which have commercial potential for developing into effective bio-pesticides. A thorough understanding of the structural and functional features of these proteases would significantly assist with targeting the design of efficient bio-control agents.

Results

Structural models of serine proteases PR1 from entomophagous fungus, Ver112 and VCP1 from nematophagous fungi, have been modeled using the homology modeling technique based on the crystal coordinate of the proteinase K. In combination with multiple sequence alignment, these models suggest one similar calcium-binding site and two common disulfide bridges in the three cuticle-degrading enzymes. In addition, the predicted mode

SUBMITTER: Liu SQ 

PROVIDER: S-EPMC1890553 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature