1gh7
From Proteopedia
CRYSTAL STRUCTURE OF THE COMPLETE EXTRACELLULAR DOMAIN OF THE BETA-COMMON RECEPTOR OF IL-3, IL-5, AND GM-CSF
Structural highlights
DiseaseIL3RB_HUMAN Defects in CSF2RB are the cause of pulmonary surfactant metabolism dysfunction type 5 (SMDP5) [MIM:614370. SMDP5 is a rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress.[1] FunctionIL3RB_HUMAN High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe receptor systems for the hemopoietic cytokines GM-CSF, IL-3, and IL-5 consist of ligand-specific alpha receptor subunits that play an essential role in the activation of the shared betac subunit, the major signaling entity. Here, we report the structure of the complete betac extracellular domain. It has a structure unlike any class I cytokine receptor described thus far, forming a stable interlocking dimer in the absence of ligand in which the G strand of domain 1 hydrogen bonds into the corresponding beta sheet of domain 3 of the dimer-related molecule. The G strand of domain 3 similarly partners with the dimer-related domain 1. The structure provides new insights into receptor activation by the respective alpha receptor:ligand complexes. Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration.,Carr PD, Gustin SE, Church AP, Murphy JM, Ford SC, Mann DA, Woltring DM, Walker I, Ollis DL, Young IG Cell. 2001 Jan 26;104(2):291-300. PMID:11207369[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Carr PD | Church AP | Ford SC | Gustin SE | Mann DA | Murphy JM | Ollis DL | Walker I | Woltring DM | Young IG
