2a4i

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

HOMOLOGY MODEL OF VIMELYSIN

spinqualitylabelsall models 2a4i Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed Vimelysin is a metalloproteinase with high activity at low temperature and an unusual resistance to organic solvents. Substrate specificities of vimelysin and thermolysin were examined using FRETS-libraries, revealing a significant difference at the P3' position: vimelysin preferred acidic amino acid residues, whereas thermolysin preferred basic residues. Homology modeling of vimelysin suggests that oppositely charged residues in the S3' subsites (R215 in vimelysin and D213 in thermolysin) may be responsible for this specificity difference. This hypothesis was confirmed by examining the R215D mutant of vimelysin, which showed a substrate specificity profile intermediate between thermolysin and vimelysin. Exploring the subsite-structure of vimelysin and thermolysin using FRETS-libraries.,Oda K, Takahashi T, Takada K, Tsunemi M, Ng KK, Hiraga K, Harada S FEBS Lett. 2005 Sep 12;579(22):5013-8. PMID:16139276 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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