Dynamic Analysis of GH Receptor Conformational Changes by Split Luciferase Complementation

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 kin...

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Bibliographische Detailangaben
Hauptverfasser: Liu, Ying, Berry, Philip A., Zhang, Yue, Jiang, Jing, Lobie, Peter E., Paulmurugan, Ramasamy, Langenheim, John F., Chen, Wen Y., Zinn, Kurt R., Frank, Stuart J.
Format: Artigo
Sprache:Inglês
Veröffentlicht: Endocrine Society 2014
Schlagworte:
Original Research
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC4213363/
https://ncbi.nlm.nih.gov/pubmed/25188449
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1210/me.2014-1153
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