دورية أكاديمية
أعرض في EDS

Modulating binding affinity, specificity, and configurations by multivalent interactions.

التفاصيل البيبلوغرافية
العنوان: Modulating binding affinity, specificity, and configurations by multivalent interactions.
المؤلفون: Deng Y; Mechanobiology Institute, National University of Singapore, Singapore., Efremov AK; Mechanobiology Institute, National University of Singapore, Singapore., Yan J; Mechanobiology Institute, National University of Singapore, Singapore; Department of Physics, National University of Singapore, Singapore. Electronic address: phyyj@nus.edu.sg.
المصدر: Biophysical journal [Biophys J] 2022 May 17; Vol. 121 (10), pp. 1868-1880. Date of Electronic Publication: 2022 Apr 20.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1542-0086 (Electronic) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
أسماء مطبوعة: Publication: Cambridge, MA : Cell Press
Original Publication: New York, Published by Rockefeller University Press [etc.] for the Biophysical Society.
مواضيع طبية MeSH: Proteins*, Binding Sites ; Ligands ; Protein Binding
مستخلص: Biological functions of proteins rely on their specific interactions with binding partners. Many proteins contain multiple domains, which can bind to their targets that often have more than one binding site, resulting in multivalent interactions. While it has been shown that multivalent interactions play a crucial role in modulating binding affinity and specificity, other potential effects of multivalent interactions are less explored. Here, we developed a broadly applicable transfer-matrix formalism and used it to investigate the binding of two-domain ligands to targets with multiple binding sites. We show that 1) ligands with two specific binding domains can drastically boost both the binding affinity and specificity and downshift the working concentration range, compared with single-domain ligands, 2) the presence of a positive domain-domain cooperativity or containing a nonspecific binding domain can downshift the working concentration range of ligands by increasing the binding affinity without compromising the binding specificity, and 3) the configuration of the bound ligands has a strong concentration dependence, providing important insights into the physical origin of phase-separation processes taking place in living cells. In line with previous studies, our results suggest that multivalent interactions are utilized by cells for highly efficient regulation of target binding involved in a diverse range of cellular processes such as signal transduction, gene transcription, and antibody-antigen recognition.
(Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.)
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المشرفين على المادة: 0 (Ligands)
0 (Proteins)
تواريخ الأحداث: Date Created: 20220422 Date Completed: 20220520 Latest Revision: 20230612
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC9199096
DOI: 10.1016/j.bpj.2022.04.017
PMID: 35450827
قاعدة البيانات: MEDLINE
الوصف
تدمد:1542-0086
DOI:10.1016/j.bpj.2022.04.017