Article
NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramer.
Biochemistry - 12 Sept 1995
Mayo K H, Roongta V, Ilyina E, Milius R, Barker S, Quinlan C, La Rosa G, Daly T J
Abstract excerpt
Native human platelet factor 4 (PF4) is a homotetrameric protein (70 residues/subunit) known for its anticoagulant heparin binding activity. 2D 15N--1H HSQC NMR experiments of native PF4 in solution show the presence of conformational heterogeneity consistent with the formation of asymmetric homo...
Topics
- Amino Acid Sequence
- Animals
- Biopolymers
- Cattle
- Computer Simulation
- Crystallography, X-Ray
- Heparin
- Humans
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Platelet Factor 4
- Protein Binding
- Protein Conformation
- Recombinant Fusion Proteins
- Solutions