Structure of Full-Length Human PDGFRβ Bound to Its Activating Ligand PDGF-B as Determined by Negative-Stain Electron Microscopy
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- 作者：Po-Han Chen1 ; Vinzenz Unger2 ; 3 ; Xiaolin He1 ; x-he@northwestern.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：ECD ; extracellular domain ; EDTA ; ethylenediaminetetraacetic acid ; EM ; electron microscopy ; FSEC ; fluorescence-coupled size-exclusion chromatography ; LMNG ; lauryl maltose neopentyl glycol ; M-CSF1 ; macrophage colony-stimulating factor 1 ; MDFF ; molecular dynamics/flexible fitting ; PDGF ; platelet-derived growth factor ; PDGFR ; PDGF receptor ; RCT ; random conical tilt ; RTK ; receptor tyrosine kinase ; SAXS ; small-angle X-ray scattering ; SCF ; stem cell factor ; sfEGFP ; superfolder enhanced green fluorescen
- 刊名：Journal of Molecular Biology
- 出版年：2015
- 出版时间：4 December 2015
- 年：2015
- 卷：427
- 期：24
- 页码：3921-3934
- 全文大小：1341 K
文摘
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Full-length transmembrane RTK structures are currently lacking.
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Purification and visualization of platelet-derived growth-factor-stimulated full-length PDGFRβ by electron microscopy.
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Domain organizations that differ from crystal structures of soluble domains.
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Asymmetric kinase domain dimer arrangement in full-length receptor.
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Demonstration of extracellular coupling with intracellular kinase activation.