Crystal Structure of the GluR2 Amino-Terminal Domain Provides Insights into the Architecture and Assembly of Ionotropic Glutamate Receptors

2009 ◽  
Vol 392 (5) ◽  
pp. 1125-1132 ◽  
Author(s):  
Amber Clayton ◽  
Christian Siebold ◽  
Robert J.C. Gilbert ◽  
Geoffrey C. Sutton ◽  
Karl Harlos ◽  
...  
2010 ◽  
Vol 78 (4) ◽  
pp. 535-549 ◽  
Author(s):  
Kasper B. Hansen ◽  
Hiro Furukawa ◽  
Stephen F. Traynelis

Cell ◽  
1996 ◽  
Vol 87 (7) ◽  
pp. 1285-1294 ◽  
Author(s):  
Theresa R Gamble ◽  
Felix F Vajdos ◽  
Sanghee Yoo ◽  
David K Worthylake ◽  
Megan Houseweart ◽  
...  

2009 ◽  
Vol 28 (12) ◽  
pp. 1812-1823 ◽  
Author(s):  
Rongsheng Jin ◽  
Satinder K Singh ◽  
Shenyan Gu ◽  
Hiroyasu Furukawa ◽  
Alexander I Sobolevsky ◽  
...  

2015 ◽  
Vol 71 (8) ◽  
pp. 1067-1071 ◽  
Author(s):  
Ji Huang ◽  
Manpreet Malhi ◽  
Jan Deneke ◽  
Marie Elizabeth Fraser

Pig GTP-specific succinyl-CoA synthetase is an αβ-heterodimer. The crystal structure of the complex with the substrate CoA was determined at 2.1 Å resolution. The structure shows CoA bound to the amino-terminal domain of the α-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides.


10.1038/11097 ◽  
1999 ◽  
Vol 1 (3) ◽  
pp. 175-182 ◽  
Author(s):  
Andrew P. May ◽  
Kira M. S. Misura ◽  
Sidney W. Whiteheart ◽  
William I. Weis

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