Unknown

Dataset Information

0

Relaxin family peptides: structure-activity relationship studies.


ABSTRACT: The human relaxin peptide family consists of seven cystine-rich peptides, four of which are known to signal through relaxin family peptide receptors, RXFP1-4. As these peptides play a vital role physiologically and in various diseases, they are of considerable importance for drug discovery and development. Detailed structure-activity relationship (SAR) studies towards understanding the role of important residues in each of these peptides have been reported over the years and utilized for the design of antagonists and minimized agonist variants. This review summarizes the current knowledge of the SAR of human relaxin 2 (H2 relaxin), human relaxin 3 (H3 relaxin), human insulin-like peptide 3 (INSL3) and human insulin-like peptide 5 (INSL5). LINKED ARTICLES:This article is part of a themed section on Recent Progress in the Understanding of Relaxin Family Peptides and their Receptors. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v174.10/issuetoc.

SUBMITTER: Patil NA 

PROVIDER: S-EPMC5406294 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Relaxin family peptides: structure-activity relationship studies.

Patil Nitin A NA   Rosengren K Johan KJ   Separovic Frances F   Wade John D JD   Bathgate Ross A D RAD   Hossain Mohammed Akhter MA  

British journal of pharmacology 20170119 10


The human relaxin peptide family consists of seven cystine-rich peptides, four of which are known to signal through relaxin family peptide receptors, RXFP1-4. As these peptides play a vital role physiologically and in various diseases, they are of considerable importance for drug discovery and development. Detailed structure-activity relationship (SAR) studies towards understanding the role of important residues in each of these peptides have been reported over the years and utilized for the des  ...[more]

Similar Datasets

| S-EPMC3975045 | biostudies-literature
| S-EPMC7667639 | biostudies-literature
| S-EPMC4773789 | biostudies-literature
| S-EPMC4278651 | biostudies-literature
| S-EPMC6855313 | biostudies-literature
| S-EPMC2932750 | biostudies-literature
| S-EPMC3963473 | biostudies-literature
| S-EPMC9142893 | biostudies-literature
| S-EPMC7498158 | biostudies-literature
| S-EPMC5846039 | biostudies-literature