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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
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Related Experiment Video

Updated: Aug 9, 2025

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering SEC-MALS
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Structural basis for membrane attack complex inhibition by CD59.

Emma C Couves1, Scott Gardner1, Tomas B Voisin1

  • 1Department of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom.

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|February 16, 2023
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Summary
This summary is machine-generated.

CD59 protein prevents cell damage by blocking membrane attack complex (MAC) pore formation. It binds complement proteins C8 and C9, halting pore assembly and protecting cells from lysis.

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • CD59 is a key regulator of the complement system, protecting host cells from damage.
  • The membrane attack complex (MAC) is a pore-forming structure that can lyse cells if not properly regulated.
  • Understanding CD59's mechanism is crucial for comprehending immune regulation and host-pathogen interactions.

Purpose of the Study:

  • To elucidate the structural mechanism by which CD59 inhibits membrane attack complex (MAC) formation.
  • To investigate the role of CD59 in preventing complement-mediated cell lysis.
  • To explore how bacterial virulence factors exploit CD59.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine structures of inhibited MAC precursors (C5b8 and C5b9).
  • Cellular assays to validate the functional consequences of CD59 binding.
  • Molecular dynamics simulations to analyze the impact of the membrane environment.

Main Results:

  • CD59 binds to the pore-forming β-hairpins of C8, forming an intermolecular β-sheet that blocks membrane insertion.
  • CD59 redirects C9 β-hairpins into the membrane, preventing MAC polymerization and pore formation.
  • Structural and cellular data reveal CD59's dual role in self-protection and its manipulation by bacterial toxins.

Conclusions:

  • CD59 effectively inhibits MAC pore formation by preventing C8 and C9 insertion and polymerization.
  • The membrane environment modulates CD59's function in complement regulation.
  • CD59 is a critical target for bacterial pathogens aiming to lyse host cells.