An improved resolution structure of the human beta 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.
Carr
P D
PD
Research School of Chemistry, Australian National University, Canberra, Australia. pdc@rsc.anu.edu.au
Conlan
F
F
Ford
S
S
Ollis
D L
DL
Young
I G
IG
D000596:Amino Acids; D001665:Binding Sites; D053648:Cytokine Receptor Common beta Subunit; D000939:Epitopes / Q000737:chemistry; D006801:Humans; D015394:Molecular Structure; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000737:chemistry*; D014961:X-Ray Diffraction
D000596:Amino Acids; C115876:CSF2RB protein, human; D053648:Cytokine Receptor Common beta Subunit; D000939:Epitopes; D011956:Receptors, Cell Surface