5K8D

Crystal structure of rFVIIIFc

Summary for 5K8D

• Entry DOI: 10.2210/pdb5k8d/pdb
• Descriptor: Coagulation factor VIII, Coagulation factor VIII,Ig gamma-1 chain C region, 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, ... (7 entities in total)
• Functional Keywords: coagulation factor, factor viii, human igg1 fc domain, hemophilia a, blood clotting
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 186530.06

Authors

Leksa, N.,Quan, C. (deposition date: 2016-05-29, release date: 2017-06-14, Last modification date: 2024-10-30)

Primary citation

Leksa, N.C.,Chiu, P.L.,Bou-Assaf, G.M.,Quan, C.,Liu, Z.,Goodman, A.B.,Chambers, M.G.,Tsutakawa, S.E.,Hammel, M.,Peters, R.T.,Walz, T.,Kulman, J.D.
The structural basis for the functional comparability of factor VIII and the long-acting variant recombinant factor VIII Fc fusion protein.
J. Thromb. Haemost., 15:1167-1179, 2017

PubMed Abstract: Essentials Recombinant factor VIII (rFVIII) Fc fusion protein has a 1.5-fold longer half-life than rFVIII. Five orthogonal methods were used to characterize the structure of rFVIIIFc compared to rFVIII. The C-terminal Fc fusion does not perturb the structure of FVIII in rFVIIIFc. The FVIII and Fc components of rFVIIIFc are flexibly tethered and functionally independent.

PubMed: 28397397
DOI: 10.1111/jth.13700

Experimental method

X-RAY DIFFRACTION (4.19 Å)