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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.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

NSP4 is found in the telomeric region of the chromosome 19.

Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights

Function

PRSS57 are granule-associated enzymes which have a function in the intracellular action against microorganisms in neutrophil cells. These enzymes is the primary reason of damages in the tissue of inflammation’s sites.

Indeed, neutrophils are rapidly recruited to the site of inflammation. Microorganisms are engulfed by the neutrophils and sequestered in the phagolysosome. This sequestration induces the fusion of neutrophil granules with the phagolysosome and the release of proteases into the phagolysosome to kill the bacteria. PRSS57 are released into specific granules, the azurophilic granules. Recent studies also show that this serine protease regulate the inflammatory response by proteolytically modifying chemokines and, activating or inactivaing cytokines. This leads to enhancement or abolishment of the function of these immune mediators. This neutrophil serine protease could also control the release of chemokines from 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.^[3]

The active is form by 4 amino acids: Gly(189), Phe(190, Ser(216), D(226) 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.