serpin

Also known as Serpins, Serpin Protease Inhibitors, Serpin Peptidase Inhibitors

Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (serine protease inhibitors). They are notable for their unusual mechanism of action, in which they irreversibly inhibit their target protease by undergoing a large conformational change to disrupt the target's active site. This contrasts with the more common competitive mechanism for protease inhibitors t

Key facts

Protein family.PDB: A:1-378 B:349-379 A:1-415 A:1-415 A:1-385 A:1-385 B:1-385 B:77-433 L:76-461 I:76-461 L:76-461 I:76-461 L:76-461 L:76-461 L:76-461 L:76-461 L:76-461 L:76-461 A:78-461 I:76-461 I:76-461p I:76-461 L:76-461 I:76-461 A:76-461 I:76-461 A:1-375 B:1-375 B:1-375 A:1-375 A:1-300 A:1-55 A:1-305 I:18-392 :18-369 :45-415 B:383-415 A:43-382 A:49-376 A:43-415 A:43-415 B:378-415 A:44-382 A:43-415 A:43-415 44-415 A:43-382 B:383-415 47-415 A:43-415 A:50-383 A:43-420 B:390-420 A:47-383 A:48-383 B:42-417 F:376-406 B:374-406 B:374-406 A:119-496 A:119-496 A:25-402 A:25-402 D:25-402 D:25-402 A:25-402 A:25-402 B:26-402 A:25-402 A:25-402 A:138-498 D:101-361 A:49-415
Protein family.Symbol: Serpin, SERPIN (root symbol of family)
Protein family.Name: Serpin (serine protease inhibitor)
Protein family.image: serpin_(stressed).png
Protein family.caption: A serpin (white) with its 'reactive centre loop' (blue) bound to a protease (grey). Once the protease attempts catalysis it will be irreversibly inhibited. ()
Protein family.Pfam: PF00079
Protein family.InterPro: IPR000215
Protein family.Prosite: PDOC00256
Protein family.SCOP: 1hle
Protein family.CDD: cd00172

via Wikipedia infobox

Research

73,110 papers

Serpin-ligand interactions.Methods (San Diego, Calif.) · 2004
Overview of serpin B9 and its roles in cancer (Review).Oncology reports · 2021
Serpin family proteins as potential biomarkers and therapeutic drugs in stroke: A systematic review and meta-analysis on clinical/preclinical studies.CNS neuroscience & therapeutics · 2023
Plant serpin protease inhibitors: specificity and duality of function.Journal of experimental botany · 2019
Serpin structures.Behring Institute Mitteilungen · 1993

via PubMed

Wikidata facts

Image: Serpin equilibrium.png

Show 1 more fact

Commons category: Serine protease inhibitors

Sources (2)

via Wikidata · CC0

~42 min read

Article

29 sections

Contents

History
Activity
Biological function and localization
Protease inhibition
Non-inhibitory roles
Structure
Conformational change and inhibitory mechanism
Allosteric activation
Latent conformation
Conformational change in non-inhibitory functions
Degradation
Disease and serpinopathies
Inactivity or absence
Specificity change
Polymerisation and aggregation
Therapeutic strategies
Evolution
Distribution
Animal
Human
Specialised mammalian serpins
Insect
Nematode
Plant
Fungal
Prokaryotic
Viral
References
External links

Protease inhibition by serpins controls an array of biological processes, including coagulation and inflammation, and consequently these proteins are the target of medical research. Their unique conformational change also makes them of interest to the structural biology and protein folding research communities. The conformational-change mechanism confers certain advantages, but it also has drawbacks: serpins are vulnerable to mutations that can result in serpinopathies such as protein misfolding and the formation of inactive long-chain polymers. Serpin polymerisation not only reduces the amount of active inhibitor, but also leads to accumulation of the polymers, causing cell death and organ failure.