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
- John Curtin School of Medical Research, Australian National University, Canberra (Australia)
- Research School of Chemistry, Australian National University, Canberra (Australia)
Data to a maximum of 2.7 Å resolution have allowed a more accurate model of the extracellular domains of the β common cytokine receptor to be determined. Structural details of the membrane-distal BC and FG loops of domain 4 and loops AB and EF of domain 1, which have been implicated in high-affinity binding, are much better defined, revealing a more compact functional epitope. X-ray diffraction has been used to produce and refine a model of the extracellular domains of the β 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.
- OSTI ID:
- 22360213
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 6; Other Information: PMCID: PMC2243076; PMID: 16754968; PUBLISHER-ID: be5056; OAI: oai:pubmedcentral.nih.gov:2243076; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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