Serpin domain (IPR023796)

Short name: Serpin_dom

Overlapping homologous superfamilies

Domain relationships


Serpins (SERine Proteinase INhibitors) belong to MEROPS inhibitor family I4, clan ID. Most serpin family members are indeed serine protease inhibitors, but several have additional cross-class inhibition functions and inhibit cysteine protease family members such as the caspases and cathepsins [PMID: 8034697, PMID: 7851535]. Others, such as ovalbumin, are incapable of protease inhibition and serve other functions [PMID: 8417965].

Serpins share a highly conserved core structure that is critical for their functioning as serine protease inhibitors [PMID: 21781239]. Inhibitory serpins comprise several alpha-helix and beta-strands together with an external reactive centre loop (RCL) containing the active site recognised by the target enzyme. Serpins form covalent complexes with target proteases. Their mechanism of protease inhibition is known as irreversible "trapping" , in which a rapid conformational change traps the cognate protease in a covalent complex.

This entry represents the structural domain of serpins.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.