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Structure paper

TitleDomain organization of membrane-bound factor VIII.
Journal, issue, pagesBiopolymers, Vol. 99, Issue 7, Page 448-459, Year 2013
Publish dateApr 22, 2016
AuthorsSvetla Stoilova-McPhie / Gillian C Lynch / Steven Ludtke / B Montgomery Pettitt /
PubMed AbstractFactor VIII (FVIII) is the blood coagulation protein which when defective or deficient causes for hemophilia A, a severe hereditary bleeding disorder. Activated FVIII (FVIIIa) is the cofactor to the ...Factor VIII (FVIII) is the blood coagulation protein which when defective or deficient causes for hemophilia A, a severe hereditary bleeding disorder. Activated FVIII (FVIIIa) is the cofactor to the serine protease factor IXa (FIXa) within the membrane-bound Tenase complex, responsible for amplifying its proteolytic activity more than 100,000 times, necessary for normal clot formation. FVIII is composed of two noncovalently linked peptide chains: a light chain (LC) holding the membrane interaction sites and a heavy chain (HC) holding the main FIXa interaction sites. The interplay between the light and heavy chains (HCs) in the membrane-bound state is critical for the biological efficiency of FVIII. Here, we present our cryo-electron microscopy (EM) and structure analysis studies of human FVIII-LC, when helically assembled onto negatively charged single lipid bilayer nanotubes. The resolved FVIII-LC membrane-bound structure supports aspects of our previously proposed FVIII structure from membrane-bound two-dimensional (2D) crystals, such as only the C2 domain interacts directly with the membrane. The LC is oriented differently in the FVIII membrane-bound helical and 2D crystal structures based on EM data, and the existing X-ray structures. This flexibility of the FVIII-LC domain organization in different states is discussed in the light of the FVIIIa-FIXa complex assembly and function.
External linksBiopolymers / PubMed:23616213 / PubMed Central
MethodsEM (helical sym.) / EM (electron crystallography)
Resolution15.0 Å
Structure data

EMDB-5540:
3D membrane-bound structure of FVIII bound to single lipid bilayer nanotubes
Method: EM (helical sym.) / Resolution: 15.0 Å

5559

3j2s

EMDB-5559: Cryo-em map of one molecule of factor VIII light chain from helically organized factor VIII light chain molecules bound to lipid nanotubes
PDB-3j2s: Membrane-bound factor VIII light chain
Method: EM (helical sym.) / Resolution: 15.0 Å

PDB-3j2q:
Model of membrane-bound factor VIII organized in 2D crystals
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 15.0 Å

Chemicals

ChemComp-CU:
COPPER (II) ION / Copper

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • homo sapiens (human)
KeywordsBLOOD CLOTTING / blood coagulation / cofactor / factor VIII / hemophilia / membrane binding

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