Transmembrane protease serine 2

Protease activity

TMPRSS2, as a serine protease, cleaves peptide bonds present after positively charged residues (lysine or arginine). The main player in the catalytic mechanism is the catalytic triad formed by His296, Asp345, and Ser441. This three aminoacids are located in the active site of the enzyme. ^[2]

The substrate specificity is achieved with the presence of a negatively charged Asp residue at the bottom of a cavity usually indicated as “S1 specificity pocket”. ^[3]

General function

In terms of normal function, TMPRSS2 has been associated with physiological and pathological processes such as digestion, tissue remodelling, blood coagulation, fertility, inflammatory responses, tumour cell invasion, apoptosis and pain. ^[4]

Prostate cancer

Viral entry

Structure

Gene

The TMPRSS2 gene resides on chromosome 21 at the band 21q22.3, and is split into 15 exons. It has an open reading frame of 492 amino acids.

This gene is conserved in a wide variety of animals, such as chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, Caenorhabditis elegans and frog.

Protein

TPMRSS2 is defined by the presence of an N-terminal cytoplasmic domain, a transmembrane helical domain, and three extracellular domains: ^[5]

• Low-density lipoprotein (LDL)-receptor class A domain
• Scavenger receptor cysteine-rich domain (SRCR)
• Peptidase S1 domain, also known as serine protease domain (SPD)

Expression

Phamacological therapeutic approaches

Structural highlights

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