Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure.
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.
van den Akker
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Department of Molecular Biology and Center for Structural Biology, Lerner Research Institute, Cleveland Clinic Foundation, OH 44195, USA. vandenf@ccf.org
D000818:Animals; D009320:Atrial Natriuretic Factor / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D011487:Protein Conformation; D017510:Protein Folding; D017461:Receptors, Atrial Natriuretic Factor / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction
D009320:Atrial Natriuretic Factor; D017461:Receptors, Atrial Natriuretic Factor