1gh7

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{{STRUCTURE_1gh7| PDB=1gh7 | SCENE= }}
{{STRUCTURE_1gh7| PDB=1gh7 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE COMPLETE EXTRACELLULAR DOMAIN OF THE BETA-COMMON RECEPTOR OF IL-3, IL-5, AND GM-CSF'''
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===CRYSTAL STRUCTURE OF THE COMPLETE EXTRACELLULAR DOMAIN OF THE BETA-COMMON RECEPTOR OF IL-3, IL-5, AND GM-CSF===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11207369 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11207369}}
==About this Structure==
==About this Structure==
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[[Category: Young, I G.]]
[[Category: Young, I G.]]
[[Category: Dimer of interlocking chains of fibronectin-iii domains four fibronectin-iii domains per chain]]
[[Category: Dimer of interlocking chains of fibronectin-iii domains four fibronectin-iii domains per chain]]
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Revision as of 02:16, 1 July 2008

Image:1gh7.png

Template:STRUCTURE 1gh7

CRYSTAL STRUCTURE OF THE COMPLETE EXTRACELLULAR DOMAIN OF THE BETA-COMMON RECEPTOR OF IL-3, IL-5, AND GM-CSF

Template:ABSTRACT PUBMED 11207369

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

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