scholarly journals Crystal structure of ginkbilobin-2 with homology to the extracellular domain of plant cysteine-rich receptor-like kinases

2009 ◽  
Vol 77 (1) ◽  
pp. 247-251 ◽  
Author(s):  
Takuya Miyakawa ◽  
Ken-ichi Miyazono ◽  
Yoriko Sawano ◽  
Ken-ichi Hatano ◽  
Masaru Tanokura
Keyword(s):  
Crystal Structure ◽  
Extracellular Domain

scholarly journals Crystal Structure of Human CD38 Extracellular Domain

Structure ◽  
2005 ◽  
Vol 13 (9) ◽  
pp. 1331-1339 ◽  
Author(s):  
Qun Liu ◽  
Irina A. Kriksunov ◽  
Richard Graeff ◽  
Cyrus Munshi ◽  
Hon Cheung Lee ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Extracellular Domain

scholarly journals Crystal Structure of the Sema-PSI Extracellular Domain of Human RON Receptor Tyrosine Kinase

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e41912 ◽  
Author(s):  
Kinlin L. Chao ◽  
I-Wei Tsai ◽  
Chen Chen ◽  
Osnat Herzberg
Keyword(s):  
Crystal Structure ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Extracellular Domain ◽  
Ron Receptor

scholarly journals Crystal Structure of the Navβ4 Extracellular Domain

2014 ◽  
Vol 106 (2) ◽  
pp. 37a
Author(s):  
Samir Das ◽  
John Gilchrist ◽  
Frank Bosmans ◽  
Filip Van Petegem
Keyword(s):  
Crystal Structure ◽  
Extracellular Domain

scholarly journals Crystal Structure of the Extracellular Domain of Mouse RANK Ligand at 2.2-Å Resolution

2001 ◽  
Vol 277 (8) ◽  
pp. 6631-6636 ◽  
Author(s):  
Shuichiro Ito ◽  
Kenji Wakabayashi ◽  
Osamu Ubukata ◽  
Shinko Hayashi ◽  
Fumihiko Okada ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Extracellular Domain ◽  
Rank Ligand

The Crystal Structure of the Extracellular Domain of Human Tissue Factor Refined to 1.7 Å Resolution

1996 ◽  
Vol 256 (1) ◽  
pp. 144-159 ◽  
Author(s):  
Yves A. Muller ◽  
Mark H. Ultsch ◽  
Abraham M. de Vos
Keyword(s):  
Crystal Structure ◽  
Tissue Factor ◽  
Human Tissue ◽  
Extracellular Domain

scholarly journals Crystal structure of a human neuronal nAChR extracellular domain in pentameric assembly: Ligand-bound α2 homopentamer

2016 ◽  
Vol 113 (34) ◽  
pp. 9635-9640 ◽  
Author(s):  
Nikolaos Kouvatsos ◽  
Petros Giastas ◽  
Dafni Chroni-Tzartou ◽  
Cornelia Poulopoulou ◽  
Socrates J. Tzartos
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Structural Information ◽  
Extracellular Domain ◽  
Binding Pocket ◽  
Nachr Subunit ◽  
Homologous Proteins ◽  
High Sequence Identity ◽  
Neuronal Nachr ◽  
Low Sensitivity

In this study we report the X-ray crystal structure of the extracellular domain (ECD) of the human neuronal α2 nicotinic acetylcholine receptor (nAChR) subunit in complex with the agonist epibatidine at 3.2 Å. Interestingly, α2 was crystallized as a pentamer, revealing the intersubunit interactions in a wild type neuronal nAChR ECD and the full ligand binding pocket conferred by two adjacent α subunits. The pentameric assembly presents the conserved structural scaffold observed in homologous proteins, as well as distinctive features, providing unique structural information of the binding site between principal and complementary faces. Structure-guided mutagenesis and electrophysiological data confirmed the presence of the α2(+)/α2(−) binding site on the heteromeric low sensitivity α2β2 nAChR and validated the functional importance of specific residues in α2 and β2 nAChR subunits. Given the pathological importance of the α2 nAChR subunit and the high sequence identity with α4 (78%) and other neuronal nAChR subunits, our findings offer valuable information for modeling several nAChRs and ultimately for structure-based design of subtype specific drugs against the nAChR associated diseases.

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