6MF2

Improved Model of Human Coagulation Factor VIII

Summary for 6MF2

• Entry DOI: 10.2210/pdb6mf2/pdb
• Related: 2R7E 6MF0
• Descriptor: Coagulation factor VIII, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: factor viii, hemophilia a, hemostasis, secreted, blood clotting
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 1
• Total formula weight: 175837.85

Authors

Smith, I.W.,Spiegel, P.C. (deposition date: 2018-09-08, release date: 2019-09-11, Last modification date: 2020-07-29)

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 (3.6093641312 Å)