Dynamic Analysis of GH Receptor Conformational Changes by Split Luciferase Complementation
Abstract
The transmembrane GH receptor (GHR) exists at least in part as a preformed homodimer on the cell surface. Structural and biochemical studies suggest that GH binds GHR in a 1:2 stoichiometry to effect acute GHR conformational changes that trigger the activation of the receptor-associated tyrosine kinase, Janus kinase 2 (JAK2), and downstream signaling. Despite information about GHR-GHR association derived from elegant fluorescence resonance...
Paper Details
Title
Dynamic Analysis of GH Receptor Conformational Changes by Split Luciferase Complementation
Published Date
Nov 1, 2014
Journal
Volume
28
Issue
11
Pages
1807 - 1819
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