echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Biochemistry News > Biotechnology News > Advances in the structure and function of glucagon-like peptide-1 receptors.

    Advances in the structure and function of glucagon-like peptide-1 receptors.

    • Last Update: 2020-08-09
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com
    On June 15th, a team of two teams from the Shanghai Institute of Pharmacy of the Chinese Academy of Sciences and the Institute of Pharmacology at Monash University in Australia published the study of two distinct domains of the glucagon-like peptide-1 receptor-peptide-mediated-biasenism in The Journal of Biology.
    G protein conjugate receptor is a family of membrane proteins with seven transmembrane structures, glucagon-like peptide-1 receptors belong to the B1 type, for the treatment of type 2 diabetes and obesity, has been listed in the receptor excited drugs including eseninatide, liraglutide and dalate, such as nearly ten, annual sales of more than 10 billion U.S. dollars.
    the different frequency, clinical efficacy, adverse reactions and tolerances shown by these drugs were closely related to the bias exagoglyceeffect effect of glucagon-like peptide-1.
    bias agoginiation refers to the binding of different agonists and receptors to make different changes in their composition and to conjugate different effect proteins, thus activating different signaling pathways or preferences to activate a signaling pathway, which in turn produces different biological effects.
    the N-end of the glucagon-like peptide-1 receptor and the first transmembrane helical near-cell outer domain in its activation process are dynamically changing and extremely unstable, and are missing in many parsed crystals or frozen electron mirror s3D structures, and there is a lack of understanding of the role of related amino acid sites.
    in order to break through this problem, the Shanghai Drug Institute's Wang Mingwei team and the Australian Monash University Patrick Sexton and Denise Wootten team began three years ago to organize a joint attack, the receptor N end and the first transmembrane helix near-cell domain of 28 amino acids fixed-point mutation, using a variety of technical systems to study the activation of a variety of peptide ligands to receptors and forces and different signal ingestive pathways (cAMP, pERK1/2 and Ca2. The results of the
    show that the different amino acid sites on the pancreatic glycemic peptide-1 receptor regulate the affinity of the ligand and the signaling pathways it activates, and there are common already characteristics between the ligands and between the signaling pathways, indicating that the domain plays an important role in regulating signal bias transduction, thus providing a new way of thinking for the design of beneficial harm-avoiding drugs based on the principle of receptor bias agitation.
    the research was supported by the Australian National Health and Medical Research Council, the National Natural Science Foundation, the Chinese Academy of Sciences Strategic Pilot Science and Technology Special And Shanghai Science and Technology Development Fund, and the first author of the paper, Wang Mingwei, a doctoral student, lei Saifei, went to Australia to study with the support of the Joint Training Program of Doctoral Students of the Chinese Academy of Sciences.
    .
    This article is an English version of an article which is originally in the Chinese language on echemi.com and is provided for information purposes only. This website makes no representation or warranty of any kind, either expressed or implied, as to the accuracy, completeness ownership or reliability of the article or any translations thereof. If you have any concerns or complaints relating to the article, please send an email, providing a detailed description of the concern or complaint, to service@echemi.com. A staff member will contact you within 5 working days. Once verified, infringing content will be removed immediately.

    Contact Us

    The source of this page with content of products and services is from Internet, which doesn't represent ECHEMI's opinion. If you have any queries, please write to service@echemi.com. It will be replied within 5 days.

    Moreover, if you find any instances of plagiarism from the page, please send email to service@echemi.com with relevant evidence.