An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope
Copyright policy )An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope
X-ray diffraction has been used to produce and refine a model of the extracellular domains of the beta common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.
- Australian National University Australia
epitope, Binding Sites, Molecular Structure, CSF2RB protein, binding site, X ray diffraction, Protein Conformation, article, cell surface receptor, Receptors, Cell Surface, chemistry, Epit, Cytokine Receptor Common beta Subunit, Epitopes, Keywords: amino acid, X-Ray Diffraction, protein conformation, CD131 antigen, chemical structure, Humans, human, Amino Acids
epitope, Binding Sites, Molecular Structure, CSF2RB protein, binding site, X ray diffraction, Protein Conformation, article, cell surface receptor, Receptors, Cell Surface, chemistry, Epit, Cytokine Receptor Common beta Subunit, Epitopes, Keywords: amino acid, X-Ray Diffraction, protein conformation, CD131 antigen, chemical structure, Humans, human, Amino Acids
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