1gh7
From Proteopedia
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CRYSTAL STRUCTURE OF THE COMPLETE EXTRACELLULAR DOMAIN OF THE BETA-COMMON RECEPTOR OF IL-3, IL-5, AND GM-CSF
Overview
The 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.
About this Structure
1GH7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 17:05:19 2007
