These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The role of glutamic acid 73 in adrenomedullin interactions with rodent AM2 receptors.
    Author: Halim A, Hay DL.
    Journal: Peptides; 2012 Jul; 36(1):137-41. PubMed ID: 22546239.
    Abstract:
    Adrenomedullin (AM) is a peptide, which is important for vascular development. There is much interest in the clinical potential of its receptors. The mode of AM binding to its receptors is poorly understood. Previous studies have identified amino acid Glu74, which is found in the receptor activity-modifying protein (RAMP3) subunit of the AM(2) receptor as important for high affinity AM interactions with this receptor. Its reciprocal residue in RAMP1 (Trp) impedes AM interactions in the closely related human calcitonin gene-related peptide (CGRP) receptor. The Glu is conserved in RAMP3 across species, supporting its role in contributing to AM binding. We mutated this residue in rat and mouse RAMP3 to Ala, Lys and Trp to determine its function in rodent AM(2) receptors. Only the Trp substitution in mouse RAMP3 produced a substantial reduction in AM potency. However, mutation of the Lys found in rat RAMP1 to Glu enhanced AM potency. Although Glu is highly conserved in RAMP3, this work suggests that it may only make a small or indirect contribution to AM interactions. Nevertheless, the equivalent amino acid in RAMP1 may serve to impair high affinity AM interactions.
    [Abstract] [Full Text] [Related] [New Search]