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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.

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Related Experiment Video

Updated: Jun 1, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
12:24

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

Functional mapping of factor VIII C2 domain.

Jean-Luc Pellequer1, Shu-wen W Chen, Didier Saboulard

  • 1CEA, iBEB, Service de Biochimie et Toxicologie Nucléaire, Bagnols sur Cèze, France. France;plantierj@lfb.fr

Thrombosis and Haemostasis
|May 27, 2011
PubMed
Summary

This study functionally mapped the factor VIII (FVIII) C2 domain by creating 139 alanine mutants. Key residues crucial for FVIII structure, function, and stability were identified, aiding recombinant FVIII development.

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Last Updated: Jun 1, 2026

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Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay
13:08

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay

Published on: September 9, 2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Factor VIII (FVIII) is essential for blood coagulation.
  • The FVIII C2 domain mediates interactions with von Willebrand factor and phospholipids.
  • Understanding C2 domain residue function is critical for FVIII structure and activity.

Purpose of the Study:

  • To comprehensively map the functional importance of each residue within the FVIII C2 domain.
  • To identify residues critical for FVIII structure, stability, and procoagulant activity.
  • To correlate functional data with structural information for targeted FVIII engineering.

Main Methods:

  • Generated 139 alanine mutants across the FVIII C2 domain (residues 2173-2325).
  • Expressed mutants in COS-1 cells and measured antigen levels and procoagulant activity.
  • Performed in silico analyses (sliding average, mutation energy cost) and correlated with experimental data.

Main Results:

  • Identified key residues essential for maintaining C2 domain structure, particularly those in β-sheets.
  • Distinguished residues critical for function from those amenable to substitution.
  • In silico analyses aligned with functional data, predicting residue importance.
  • Established detailed functional relationships with crystallographic data.

Conclusions:

  • Provided a comprehensive functional map of the FVIII C2 domain.
  • Highlighted the implications of specific residues for FVIII activity, stability, secretion, and phospholipid binding.
  • Demonstrated the utility of combined functional and in silico approaches for engineering recombinant FVIII molecules.