Receptor Activity Modification Protein 3, also known as RAMP3, is a protein which is encoded by RAMP3 gene. It is also named as Calcitonin-receptor-like receptor activity-modifying protein 3 (CRLR activity-modifying protein 3). The RAMP3 is a member of the RAMPs family of single-transmembrane domain proteins. Ramps are type I transmembrane proteins with an extracellular N-terminus and a cytoplasmic C-terminus. CRLR is a receptor with seven transmembrane domains that can act as a calcitonin gene-related peptide (CGRP) receptor or adrenergic receptor, depending on how members of the RAMP family are expressed. In humans and other mammals, there are 3 RAMPS, and in fish, there are more sub-mutations. In the presence of this (RAMP3) protein, CRLR acts as an adrenergic receptor with a lower affinity for CGRP.
|Basic Information of RAMP3|
|Protein Name||Receptor activity-modifying protein 3|
|Aliases||Calcitonin-receptor-like receptor activity-modifying protein 3 (CRLR activity-modifying protein 3)|
|Organism||Homo sapiens (Human)|
The RAMP family consists of three proteins (RAMPs 1-3) that share similar molecular mass (160 amino acids) and structure, but the requirements for sequence homology, tissue distribution, and normal embryo development vary. RAMP3 is caused by estrogen, which contains a functional estrogen receptor response element in its promoter. Ramps are required to transport the calcitonin-receptor (CRLR) receptor (CRLR) onto the plasma membrane.
Fig.1 The structure of Receptor activity-modifying protein 3.
This study shows that ADM increases the association between CALCL and RAMP3, while the knockout of RAMP3 suppresses the interaction between ADM and CALCRL.
These results indicate that the interaction of RAMP2 or RAMP3 with CLR induces conformational variation in the juxtamembrane region, yielding distinct binding pockets, probably via an allosteric mechanism.
These results indicate that in the membrane proximal region, the interaction of RAMP2 or RAMP3 and CLR results in a conformational change in the membrane proximal region, resulting in a distinct binding pocket, possibly through an allosteric mechanism.
The study reveals that compared to RAMP1 and RAMP2, the role of RAMP3's specific residue on the clr-RAMP interface seems to change.
These data show the dependence of RAMP3 in the context of chronic hypertension, sexual dependence, cardiovascular protection.
To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-RAMP3 antibody development services.
Creative Biolabs' skillful scientists are glad to leverage our expertise and advanced technologies to help you with the member protein research. If you are interested, please feel free to contact us for more details.