Structural Basis for Regulation of GPR56/ADGRG1 by Its Alternatively Spliced Extracellular Domains

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Structural Basis for Regulation of GPR56/ADGRG1 by Its Alternatively Spliced Extracellular Domains

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作者：Gabriel S. Salzman¹ ; ² ; ³ ; Sarah D. Ackerman⁴ ; Chen Ding³ ; ⁷ ; Akiko Koide³ ; ⁸ ; Katherine Leon³ ; Rong Luo⁵ ; Hannah M. Stoveken⁶ ; Celia G. Fernandez³ ; Gregory G. Tall⁶ ; Xianhua Piao⁵ ; Kelly R. Monk⁴ ; Shohei Koide³ ; ⁸ ; ^{shohei.koide@nyumc.org" class="auth_mail" title="E-mail the corresponding author} ; Demet Araç ; ³ ; ⁹ ; ^{arac@uchicago.edu" class="auth_mail" title="E-mail the corresponding author}
关键词：oligodendrocyte development ; adhesion GPCR ; monobody ; X-ray crystallography ; protein engineering
刊名：Neuron
出版年：2016
出版时间：21 September 2016
年：2016
卷：91
期：6
页码：1292-1304
全文大小：3171 K

文摘

•: Crystal structure of the entire extracellular region of GPR56, an adhesion GPCR
•: A unique “PLL” domain interacts extensively with a smaller-than-usual GAIN domain
•: PLL acts as a damper of basal activity and supports oligodendrocyte development
•: A monobody directed to the extracellular region allosterically inhibits signaling

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