دورية أكاديمية
Diversity of Structural, Dynamic, and Environmental Effects Explain a Distinctive Functional Role of Transmembrane Domains in the Insulin Receptor Subfamily.
العنوان: | Diversity of Structural, Dynamic, and Environmental Effects Explain a Distinctive Functional Role of Transmembrane Domains in the Insulin Receptor Subfamily. |
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المؤلفون: | Bershatsky YV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Kuznetsov AS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Idiatullina AR; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Bocharova OV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Dolotova SM; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Gavrilenkova AA; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Serova OV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Deyev IE; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Rakitina TV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Zangieva OT; Federal State Budgetary Institution 'National Medical and Surgical Center named after N.I. Pirogov', Moscow 105203, Russia., Pavlov KV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Federal Clinical Center of Physical-Chemical Medicine of FMBA, Moscow 119435, Russia., Batishchev OV; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia.; Frumkin Institute of Physical Chemistry and Electrochemistry of Russian Academy of Sciences, Moscow 119071, Russia., Britikov VV; Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 220141 Minsk, Belarus., Usanov SA; Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 220141 Minsk, Belarus., Arseniev AS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Efremov RG; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia.; Department of Applied Mathematics, National Research University Higher School of Economics, Moscow 101000, Russia., Bocharov EV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia. |
المصدر: | International journal of molecular sciences [Int J Mol Sci] 2023 Feb 15; Vol. 24 (4). Date of Electronic Publication: 2023 Feb 15. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Basel, Switzerland : MDPI, [2000- |
مواضيع طبية MeSH: | Receptor, Insulin*/chemistry , Receptor, Insulin*/physiology , Drug Development*, Humans ; Protein Domains ; Signal Transduction |
مستخلص: | Human InsR, IGF1R, and IRR receptor tyrosine kinases (RTK) of the insulin receptor subfamily play an important role in signaling pathways for a wide range of physiological processes and are directly associated with many pathologies, including neurodegenerative diseases. The disulfide-linked dimeric structure of these receptors is unique among RTKs. Sharing high sequence and structure homology, the receptors differ dramatically in their localization, expression, and functions. In this work, using high-resolution NMR spectroscopy supported by atomistic computer modeling, conformational variability of the transmembrane domains and their interactions with surrounding lipids were found to differ significantly between representatives of the subfamily. Therefore, we suggest that the heterogeneous and highly dynamic membrane environment should be taken into account in the observed diversity of the structural/dynamic organization and mechanisms of activation of InsR, IGF1R, and IRR receptors. This membrane-mediated control of receptor signaling offers an attractive prospect for the development of new targeted therapies for diseases associated with dysfunction of insulin subfamily receptors. |
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معلومات مُعتمدة: | 23-44-10021 Russian Science Foundation; Х23РНФ-091 Belarusian Republican Foundation for Basic Research |
فهرسة مساهمة: | Keywords: NMR; insulin receptor subfamily; molecular dynamics; protein-lipid interactions; receptor tyrosine kinases; structural-dynamical properties; transmembrane domain |
المشرفين على المادة: | EC 2.7.10.1 (Receptor, Insulin) |
تواريخ الأحداث: | Date Created: 20230225 Date Completed: 20230329 Latest Revision: 20230329 |
رمز التحديث: | 20230331 |
مُعرف محوري في PubMed: | PMC9965288 |
DOI: | 10.3390/ijms24043906 |
PMID: | 36835322 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1422-0067 |
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DOI: | 10.3390/ijms24043906 |