Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin

2003 ◽  
Vol 10 (3) ◽  
pp. 226-231 ◽  
Author(s):  
Emiko Yamauchi ◽  
Toru Nakatsu ◽  
Mamoru Matsubara ◽  
Hiroaki Kato ◽  
Hisaaki Taniguchi
Keyword(s):  
Crystal Structure ◽  
Binding Domain ◽  
Calmodulin Binding

scholarly journals Crystal Structure of Calmodulin Binding Domain of Orai1 in Complex with Ca2+•Calmodulin Displays a Unique Binding Mode

2012 ◽  
Vol 287 (51) ◽  
pp. 43030-43041 ◽  
Author(s):  
Yanshun Liu ◽  
Xunhai Zheng ◽  
Geoffrey A. Mueller ◽  
Mack Sobhany ◽  
Eugene F. DeRose ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Mode ◽  
Binding Domain ◽  
Calmodulin Binding

scholarly journals Modulation of erythrocyte Ca2+-ATPase by selective calpain cleavage of the calmodulin-binding domain

1989 ◽  
Vol 264 (14) ◽  
pp. 8289-8296 ◽  
Author(s):  
P James ◽  
T Vorherr ◽  
J Krebs ◽  
A Morelli ◽  
G Castello ◽  
...  
Keyword(s):  
Binding Domain ◽  
Calmodulin Binding

scholarly journals The Calmodulin Binding Domain of the Plasma Membrane Ca2+ Pump Interacts Both with Calmodulin and with Another Part of the Pump

1989 ◽  
Vol 264 (21) ◽  
pp. 12313-12321 ◽  
Author(s):  
A Enyedi ◽  
T Vorherr ◽  
P James ◽  
D J McCormick ◽  
A G Filoteo ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Domain ◽  
Calmodulin Binding

Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure

2001 ◽  
Vol 79 (8) ◽  
pp. 692-704 ◽  
Author(s):  
Focco van den Akker
Keyword(s):  
Crystal Structure ◽  
Atrial Natriuretic Factor ◽  
Binding Protein ◽  
Chloride Ion ◽  
Binding Domain ◽  
Protein Fold ◽  
Hormone Binding ◽  
Periplasmic Binding Protein ◽  
Natriuretic Factor ◽  
Hormone Binding Domain

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

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