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Molecular Mechanisms of Class B GPCR Activation: Insights from Adrenomedullin Receptors.
ACS Pharmacol Transl Sci
April 2020
School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand.
Adrenomedullin (AM) is a 52 amino acid peptide that plays a regulatory role in the vasculature. Receptors for AM comprise the class B G protein-coupled receptor, the calcitonin-like receptor (CLR), in complex with one of three receptor activity-modifying proteins (RAMPs). The C-terminus of AM is involved in binding to the extracellular domain of the receptor, while the N-terminus is proposed to interact with the juxtamembranous portion of the receptor to activate signaling.
View Article and Find Full Text PDFThe Structure of the CGRP and Related Receptors.
Handb Exp Pharmacol
September 2019
School of Life and Health Science, Aston University, Birmingham, UK.
The canonical CGRP receptor is a complex between calcitonin receptor-like receptor (CLR), a family B G-protein-coupled receptor (GPCR) and receptor activity-modifying protein 1 (RAMP1). A third protein, receptor component protein (RCP) is needed for coupling to Gs. CGRP can interact with other RAMP-receptor complexes, particularly the AMY1 receptor formed between the calcitonin receptor (CTR) and RAMP1.
View Article and Find Full Text PDFHow amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus.
J Membr Biol
October 2014
Institute of Physical Biology, Heinrich Heine University, Universitätsstr. 1, 40225, Düsseldorf, Germany.
Amphipathic polymers called amphipols provide a valuable alternative to detergents for keeping integral membrane proteins soluble in aqueous buffers. Here, we characterize spatial contacts of amphipol A8-35 with membrane proteins from two architectural classes: The 8-stranded β-barrel outer membrane protein OmpX and the α-helical protein bacteriorhodopsin. OmpX is well structured in A8-35, with its barrel adopting a fold closely similar to that in dihexanoylphosphocholine micelles.
View Article and Find Full Text PDFReceptor activity-modifying protein-dependent effects of mutations in the calcitonin receptor-like receptor: implications for adrenomedullin and calcitonin gene-related peptide pharmacology.
Br J Pharmacol
February 2014
School of Biological Sciences, University of Auckland, Auckland, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand.
Background And Purpose: Receptor activity-modifying proteins (RAMPs) define the pharmacology of the calcitonin receptor-like receptor (CLR). The interactions of the different RAMPs with this class B GPCR yield high-affinity calcitonin gene-related peptide (CGRP) or adrenomedullin (AM) receptors. However, the mechanism for this is unclear.
View Article and Find Full Text PDFReceptor activity-modifying protein-dependent impairment of calcitonin receptor splice variant Δ(1-47)hCT((a)) function.
Br J Pharmacol
February 2013
School of Biological Sciences, University of Auckland, Auckland, New Zealand.
Background And Purpose: Alternative splicing expands proteome diversity to GPCRs. Distinct receptor variants have been identified for a secretin family GPCR, the calcitonin receptor (CTR). The possible functional contributions of these receptor variants are further altered by their potential interactions with receptor activity-modifying proteins (RAMPs).
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