This is a default text for your page Serine protease 57 (PRSS57). Click above on edit this page to modify. Be careful with the < and > signs.
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Function
PRSS57 are granule-associated enzymes which have a function in the intracellular action against microorganisms in neutrophil cells. These enzymes are release from activated-neutrophils and is the primary reason of damages in the tissue of inflammation’s sites.
The enzyme plays a role in the inflammatory response because of the activation of chemokines, cytokines and grow factors release. They can also act on specific receptors to prolong or inhibit cytokines-induced response and modulate activities of neutrophils.
In addition, the caspase-like activity of PRSS57 can activate lymphocytes and the adaptive immune response.
Disease
Claire
Relevance
Structural highlights
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The protein has a 283 amino-acids long sequence with two mainly domains. It forms a kind of elongate sphere of approximately 70Å large and 150Å long (dimensions: 70,37Å X 70,37Å X 105,02Å). The protein is composed of signal peptide (1-31) which leads to the location in azurophil granules [1] and allows its excretion. In addition there is a protease domain (32-283) which is a trypsin-like domain with a trypsin-like active site, according to the specificity for P1-Arg residues, but this domain can be an elastase-like active site according to the primary sequence (because of the presence of a swallow S1 pocket) specific to small aliphatic residues. [2]
The active is form by 4 amino acids: Gly(189), Phe(190, Ser(216), D(226)[3]
The residue F190 obstructs the active site which could normally not links a P1-Arg. However, a study[4] considered the possibility that the two residues S216 and F190 of the active site can form a flexible gate which allows P1-Arg to enter. Then, the link between the active site and P1-Arg can be stabilized by a salt bridge interaction between S1-D226 and P1-Arg.
The hypothesis of the flexible gate was confirmed by the same study. The mutations of S216 only, F190 only or both together show a forced full open gate is more efficient than a forced partially open gate.
The conclusion is that the protease domain is a trypsin-like domain.
