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Related Concept Videos

Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

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Updated: May 30, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

Serpin structure, function and dysfunction.

J A Huntington1

  • 1Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK. jah52@cam.ac.uk

Journal of Thrombosis and Haemostasis : JTH
|July 26, 2011
PubMed
Summary
This summary is machine-generated.

Serine protease inhibitors (serpins) share a conserved structure crucial for inhibiting proteases. Cofactors modulate serpin activity, while misfolding can cause disease, with domain-swapping potentially forming polymers.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Serpins are a protein superfamily with a conserved structure critical for serine protease inhibition.
  • Despite low sequence homology, structural similarities allow knowledge transfer across serpin family members.
  • Serpin function relies on conformational changes, making them susceptible to mutations causing deficiency and disease.

Purpose of the Study:

  • To review serpin structure and protease inhibition mechanisms.
  • To illustrate cofactor modulation of serpin activity using antithrombin (AT) data.
  • To discuss serpin polymer formation and its link to cellular accumulation.

Main Methods:

  • Review of existing crystallographic and biochemical data on antithrombin.
  • Analysis of serpin structure and conformational changes.
  • Examination of domain-swapping mechanisms in serpin polymer formation.

Main Results:

  • Serpin activity is modulated by cofactors, exemplified by antithrombin.
  • Conformational changes are essential for serpin function but can lead to misfolding and disease.
  • Crystal structures reveal serpins can form polymers via domain-swapping, explaining intracellular accumulation.

Conclusions:

  • Serpins utilize a conserved structural mechanism for protease inhibition, influenced by cofactors.
  • Misfolded serpins can lead to disease, with domain-swapping implicated in polymer formation.
  • The described mechanisms provide a general framework for understanding serpin function in haemostasis and fibrinolysis.