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Publication Abstract from PubMed

The (pro)renin receptor (PRR) is an important component of the renin-angiotensin system (RAS), which regulates blood pressure and cardiovascular function. The integral membrane protein PRR contains a large extracellular domain ( approximately 310 amino acids), a single transmembrane domain ( approximately 20 amino acids) and an intracellular domain ( approximately 19 amino acids). Although short, the intracellular (IC) domain of the PRR has functionally important roles in a number of signal transduction pathways activated by (pro)renin binding. Meanwhile, together with the transmembrane domain and a small portion of the extracellular domain ( approximately 30 amino acids), the IC domain is also involved in assembly of V(0) portion of the vacuolar proton-translocating ATPase (V-ATPase). To better understand structural and multifunctional roles of the PRR-IC, we report the crystal structure of the PRR-IC domain as maltose-binding protein (MBP) fusion proteins at 2.0A (maltose-free) and 2.15A (maltose-bound). In the two separate crystal forms having significantly different unit-cell dimensions and molecular packing, MBP-PRR-IC fusion protein was found to be a dimer, which is different with the natural monomer of native MBP. The PRR-IC domain appears as a relatively flexible loop and is responsible for the dimerization of MBP fusion protein. Residues in the PRR-IC domain, particularly two tyrosines, dominate the intermonomer interactions, suggesting a role for the PRR-IC domain in protein oligomerization.

Structural analysis of the intracellular domain of (pro)renin receptor fused to maltose-binding protein.,Zhang Y, Gao X, Michael Garavito R Biochem Biophys Res Commun. 2011 Mar 21. PMID:21420935^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.