F. Van Den Akker, Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure, CAN J PHYSL, 79(8), 2001, pp. 692-704
The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF
) receptor hormone-binding domain has provided a first structural view of t
his anti-hypertensive receptor. The structure reveals a surprising evolutio
nary link to the periplasmic-binding protein fold family. Furthermore, the
presence of a chloride ion in the membrane distal domain and the presence o
f 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 includi
ng the different binding sites for the ANF hormone, chloride ion, putative
effector pocket, glycosylation sites, and dimer interface.