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Met872 is the key residue determining the novel binominal binding of metabotropic glutamate receptor 7 to calmodulin.

Authors
  • Isozumi, Noriyoshi1
  • Ohki, Shinya2
  • 1 Center for Nano Materials and Technology (CNMT), Japan Advanced Institute of Science and Technology (JAIST), 1-1 Asahidai, Nomi, Ishikawa, 923-1292, Japan. Electronic address: [email protected] , (Japan)
  • 2 Center for Nano Materials and Technology (CNMT), Japan Advanced Institute of Science and Technology (JAIST), 1-1 Asahidai, Nomi, Ishikawa, 923-1292, Japan. , (Japan)
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
Publisher
Elsevier
Publication Date
Dec 10, 2019
Volume
520
Issue
3
Pages
640–644
Identifiers
DOI: 10.1016/j.bbrc.2019.10.053
PMID: 31627896
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Two mGluR7-derived peptides corresponding to residues 856 to 879 and 856 to 875 are known to bind to Ca2+-saturated calmodulin (Ca2+/CaM), and their binding manners are thought to differ. Met872 function is believed as one of the anchor residues for CaM-binding only in the shorter peptide. To uncover the role of Met872 in CaM-binding, we prepared a mutant of the long peptide, mGluR7 (M872A), in which Met872 was replaced with Ala. We used the mutant together with the two peptides to perform NMR-titration experiments to monitor interaction with stable isotope-labeled CaM. Interaction of Ca2+/CaM with mGluR7 (M872A) caused a spectrum that differed from that of Ca2+/CaM with the long peptide, suggesting that Met872 of mGluR7 could be involved in CaM-binding even in the long peptide. Analyses of all NMR data suggested that the binding between Ca2+/CaM and mGluR7 occurs in some conformational equilibrium manner. The unique CaM-binding properties caused by Met872 may be related to mGluR7's function. Copyright © 2019 Elsevier Inc. All rights reserved.

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