Part:BBa_K4496002
Optimized Bj46a for Pichia Pastoris
This part is an inhibitor named "BJ46a", which can be taken from the plasma of Bothrops jararaca.
Natural inhibitors for snake venoms have this name because they are taken from the serum of the snake itself, or come from mammalian tissues. As of 2014, 42 such inhibitors have been described (BASTOS, 2016).
SVMP (metalloproteases) are able to hydrolyze fibrinogen, which is a glycoprotein with an important role in blood coagulation, degrading preferentially two of the three component peptide chains of this protein. Such metalloproteases usually have determined crystallographic structures, which can facilitate the analysis of SVMP inhibitory structures, such as BJ46a.
Natural SVMP (metalloprotease) inhibitors (derived from snake serum) can be defined as acidic glycoproteins that maintain inhibition over a wide pH and temperature range. In addition, they are usually dimetric.
BJ46a is an acidic glycoprotein, with molecular mass 46 kDa, capable of inhibiting the activity of the metalloproteases jararhagin and atrolysin-C by forming non-covalent complexes with such SVMPs. Studies indicate that despite the presence of the glycidic portion in ISVMP, this portion does not present a direct relevance for its proteolytic activity (unlike other inhibitors, such as DM43), which indicates that the interaction regions between the inhibitor and toxin occur in the protein portion of the glycoprotein.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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