Crystal Structure of the Oxidized Form of the Periplasmic Mercury-binding Protein MerP from Ralstonia metallidurans CH34

2004 ◽  
Vol 339 (1) ◽  
pp. 161-171 ◽  
Author(s):  
Laurence Serre ◽  
Emmanuel Rossy ◽  
Eva Pebay-Peyroula ◽  
Claudine Cohen-Addad ◽  
Jacques Covès
2004 ◽  
Vol 337 (3) ◽  
pp. 761-770 ◽  
Author(s):  
Mutsuko Kukimoto-Niino ◽  
Kazutaka Murayama ◽  
Mio Inoue ◽  
Takaho Terada ◽  
Jeremy R.H. Tame ◽  
...  

2001 ◽  
Vol 79 (8) ◽  
pp. 692-704 ◽  
Author(s):  
Focco van den Akker

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.


1994 ◽  
Vol 13 (1) ◽  
pp. 205-212 ◽  
Author(s):  
D.W. Hoffman ◽  
C. Davies ◽  
S.E. Gerchman ◽  
J.H. Kycia ◽  
S.J. Porter ◽  
...  

1997 ◽  
Vol 16 (7) ◽  
pp. 1475-1483 ◽  
Author(s):  
H. L. Monaco

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