CALCRL: A Promising Drug Target for Calcitonin Receptor-Like (G10203)

Target Name: CALCRL

NCBI ID: G10203

CALCRL

CALCRL: A Promising Drug Target for Calcitonin Receptor-Like

Calcitonin is a well-known hormone that plays a crucial role in regulating various physiological processes in the body. It is produced by the parathyroid gland and helps maintain homeostasis by regulating calcium levels in the blood. Calcinonin receptor-like (CALCRL) is a protein that shares structural similarities with the calcium-binding adaptor protein calbindin, which is expressed in various tissues throughout the body. The identification and characterization of CALCRL as a potential drug target and biomarker for various diseases have generated significant interest in this area. In this article, we will explore the biology of CALCRL, its potential drug target status, and its implications for the future of healthcare.

Structure and Function

CALCRL is a 19 kDa protein that is expressed in various tissues, including pancreatic, thyroid, and parathyroid glands. It is composed of a N-terminus, a catalytic C-terminus, and a C-terminal tail that contains a unique N-glycosylation site. The N-terminus of CALCRL contains a putative G-protein-coupled receptor (GPCR) domain, which is responsible for its interactions with ligands. The C-terminus of CALCRL contains a calcitonin receptor-like domain (CALRD) and a carboxylic acid residue (CAR), which is involved in the formation of a covalent complex with the Calbindin protein.

Calcitonin Receptor-Like Domain

The CALCRL protein contains a calcitonin receptor-like domain (CALRD), which is responsible for its interactions with the Calbindin protein. The CALRD is a single transmembrane domain that contains a nucleotide-binding oligomerization (NBO) domain and a carboxylic acid residue (CAR). The NBO domain is responsible for the formation of a covalent complex with the Calbindin protein, which is essential for the protein's calcium-binding properties. The CAR is responsible for the formation of a covalent complex with the parathyroid hormone (PTH), which triggers the release of calcium ions from the parathyroid gland.

Drug Target Status

The potential drug target status of CALCRL is based on its structural and functional similarities to the calcium-binding adaptor protein calbindin. Both proteins contain a N-terminus that is responsible for the formation of a covalent complex with a ligand, incalenin in the case of CALCRL and PTH in the case of calbindin. Additionally, both proteins contain a C-terminus that is involved in the formation of a covalent complex with a ligand. The structural similarity between these two proteins suggests that they may share similar functions and be potential drug targets.

Calcitonin Receptor-Like as a Biomarker

The potential use of CALCRL as a biomarker for various diseases is based on its ability to interact with the Calbindin protein. The release of calcium ions from the parathyroid gland is a well-established biomarker for the diagnosis of hypocalcemia (low calcium levels), which is a common complication in various diseases, including bone loss, hypoparathyroidism, and certain cancers. The potential use of CALCRL as a biomarker for these diseases is based on the ability of the protein to interact with the Calbindin protein, which is responsible for the release of calcium ions from the parathyroid gland.

Conclusion

In conclusion, the biology and structural characteristics of CALCRL suggest that it is a promising drug target for various diseases. The potential use of the protein as a biomarker for hypocalcemia and its structural similarity to the calcium-binding adaptor protein calbindin make it an attractive candidate for further research. Further studies are needed to determine the full potential of

Protein Name: Calcitonin Receptor Like Receptor

Functions: Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 (By similarity). Receptor for adrenomedullin together with RAMP2 (PubMed:22102369, PubMed:30115739). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (PubMed:22102369, PubMed:30115739)

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