Effect of the achondroplasia mutation on FGFR3 dimerization and FGFR3 structural response to fgf1 and fgf2: A quantitative FRET study in osmotically derived plasma membrane vesicles
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- 作者：Sarvenaz Sarabipour ; Kalina Hristova kh@jhu.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Receptor tyrosine kinases ; Fibroblast growth factor receptor 3 ; Dimerization ; Achondroplasia ; skeletal disorders ; Dimer stability
- 刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：1858
- 期：7
- 页码：1436-1442
- 全文大小：976 K
文摘
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We study the effect of the G380R mutation on the early stages of FGFR3 signaling.
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The G380 mutation increased FGFR3 dimerization.
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The G380R mutation causes no measurable structural perturbations when ligands are bound.
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The structural effects of the G380 and A391E mutations are distinctly different.