دورية أكاديمية
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Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain.

التفاصيل البيبلوغرافية
العنوان: Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain.
المؤلفون: Wu A; Department of Ophthalmology, Gavin Herbert Eye Institute, University of California, Irvine, CA, 92697, USA., Salom D; Department of Ophthalmology, Gavin Herbert Eye Institute, University of California, Irvine, CA, 92697, USA., Hong JD; Department of Ophthalmology, Gavin Herbert Eye Institute, University of California, Irvine, CA, 92697, USA.; Department of Chemistry, University of California, Irvine, CA, 92697, USA., Tworak A; Department of Ophthalmology, Gavin Herbert Eye Institute, University of California, Irvine, CA, 92697, USA., Watanabe K; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, 466- 8555, Japan.; PRESTO, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama, 332-0012, Japan., Pardon E; Structural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.; VIB-VUB Center for Structural Biology, VIB, Brussels, Belgium., Steyaert J; Structural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.; VIB-VUB Center for Structural Biology, VIB, Brussels, Belgium., Kandori H; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, 466- 8555, Japan.; OptoBioTechnology Research Center, Nagoya Institute of Technology, Showa-ku, Nagoya, 466-8555, Japan., Katayama K; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, 466- 8555, Japan. katayama.kota@nitech.ac.jp.; PRESTO, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama, 332-0012, Japan. katayama.kota@nitech.ac.jp.; OptoBioTechnology Research Center, Nagoya Institute of Technology, Showa-ku, Nagoya, 466-8555, Japan. katayama.kota@nitech.ac.jp., Kiser PD; Department of Ophthalmology, Gavin Herbert Eye Institute, University of California, Irvine, CA, 92697, USA. pkiser@uci.edu.; Department of Physiology & Biophysics, University of California, Irvine, CA, USA. pkiser@uci.edu.; Department of Clinical Pharmacy Practice, University of California, Irvine, CA, USA. pkiser@uci.edu.; Research Service, VA Long Beach Healthcare System, Long Beach, CA, USA. pkiser@uci.edu., Palczewski K; Department of Ophthalmology, Gavin Herbert Eye Institute, University of California, Irvine, CA, 92697, USA. kpalczew@uci.edu.; Department of Chemistry, University of California, Irvine, CA, 92697, USA. kpalczew@uci.edu.; Department of Physiology & Biophysics, University of California, Irvine, CA, USA. kpalczew@uci.edu.; Department of Molecular Biology and Biochemistry, University of California, Irvine, CA, 92697, USA. kpalczew@uci.edu.
المصدر: Nature communications [Nat Commun] 2023 Aug 25; Vol. 14 (1), pp. 5209. Date of Electronic Publication: 2023 Aug 25.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: Single-Domain Antibodies* , Camelids, New World* , Ear Auricle*, Animals ; Rhodopsin ; Gene Library
مستخلص: Rhodopsin is a prototypical G protein-coupled receptor (GPCR) critical for vertebrate vision. Research on GPCR signaling states has been facilitated using llama-derived nanobodies (Nbs), some of which bind to the intracellular surface to allosterically modulate the receptor. Extracellularly binding allosteric nanobodies have also been investigated, but the structural basis for their activity has not been resolved to date. Here, we report a library of Nbs that bind to the extracellular surface of rhodopsin and allosterically modulate the thermodynamics of its activation process. Crystal structures of Nb2 in complex with native rhodopsin reveal a mechanism of allosteric modulation involving extracellular loop 2 and native glycans. Nb2 binding suppresses Schiff base deprotonation and hydrolysis and prevents intracellular outward movement of helices five and six - a universal activation event for GPCRs. Nb2 also mitigates protein misfolding in a disease-associated mutant rhodopsin. Our data show the power of nanobodies to modulate the photoactivation of rhodopsin and potentially serve as therapeutic agents for disease-associated rhodopsin misfolding.
(© 2023. Springer Nature Limited.)
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معلومات مُعتمدة: P30 EY034070 United States EY NEI NIH HHS; I01 BX004939 United States BX BLRD VA; R01 EY034519 United States EY NEI NIH HHS; P30 GM124165 United States GM NIGMS NIH HHS; F30 EY033659 United States EY NEI NIH HHS; P41 GM103393 United States GM NIGMS NIH HHS
المشرفين على المادة: 9009-81-8 (Rhodopsin)
0 (Single-Domain Antibodies)
تواريخ الأحداث: Date Created: 20230825 Date Completed: 20230828 Latest Revision: 20240212
رمز التحديث: 20240212
مُعرف محوري في PubMed: PMC10457330
DOI: 10.1038/s41467-023-40911-9
PMID: 37626045
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-023-40911-9