6MF0

Crystal Structure Determination of Human/Porcine Chimera Coagulation Factor VIII

Summary for 6MF0

• Entry DOI: 10.2210/pdb6mf0/pdb
• Related: 6MF2
• Descriptor: Coagulation factor VIII chimera, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: hemostasis, hemophilia a, factor viii, chimera, blood clotting
• Biological source: Sus scrofa (Pig); More
• Total number of polymer chains: 2
• Total formula weight: 342564.29

Authors

Smith, I.W.,Spiegel, P.C. (deposition date: 2018-09-07, release date: 2019-09-11, Last modification date: 2024-10-23)

Primary citation

Smith, I.W.,d'Aquino, A.E.,Coyle, C.W.,Fedanov, A.,Parker, E.T.,Denning, G.,Spencer, H.T.,Lollar, P.,Doering, C.B.,Spiegel Jr., P.C.
The 3.2 angstrom structure of a bioengineered variant of blood coagulation factor VIII indicates two conformations of the C2 domain.
J.Thromb.Haemost., 18:57-69, 2020

PubMed Abstract: Coagulation factor VIII represents one of the oldest protein-based therapeutics, serving as an effective hemophilia A treatment for half a century. Optimal treatment consists of repeated intravenous infusions of blood coagulation factor VIII (FVIII) per week for life. Despite overall treatment success, significant limitations remain, including treatment invasiveness, duration, immunogenicity, and cost. These issues have inspired research into the development of bioengineered FVIII products and gene therapies.

PubMed: 31454152
DOI: 10.1111/jth.14621

Experimental method

X-RAY DIFFRACTION (3.19999885698 Å)