Calmodulin complexes with brain and muscle creatine kinase peptides
| Autor: | Leila Lo Leggio, J. Sprenger, Emad Tajkhorshid, Ashley Vanderbeck, Jenny Bredfelt, Neal Patel, Sara Linse, Karin S. Åkerfeldt, Roger S. Rowlett, Anda Trifan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Gene isoform
Cell signaling Fmoc Fluorenylmethoxycarbonyl Calmodulin QH301-705.5 CKB Creatine kinase brain-type Peptide CrP Creatine phosphate Article Cellular energy metabolism Calmodulin X-ray structure ADP Adenosine diphosphate Cr Creatine Structural Biology ddc:570 CaM Calmodulin Biology (General) Molecular Biology Enzyme regulation Calcium signaling chemistry.chemical_classification biology Isothermal titration calorimetry CK Creatine kinase CKM Creatine kinase muscle-type Enzyme chemistry MR Molecular replacement Biophysics biology.protein PDB Protein data bank ATP Adenosine triphosphate Creatine kinase ITC Isothermal titration calorimetry Ca2+ Calcium ion (divalent) |
| Zdroj: | 'Current Research in Structural Biology ', vol: 3, pages: 121-132 (2021) Current Research in Structural Biology, Vol 3, Iss, Pp 121-132 (2021) Current research in structural biology 3, 121-132 (2021). doi:10.1016/j.crstbi.2021.05.001 Current Research in Structural Biology Sprenger, J, Trifan, A, Patel, N, Vanderbeck, A, Bredfelt, J, Tajkhorshid, E, Rowlett, R, Lo Leggio, L, Åkerfeldt, K S & Linse, S 2021, ' Calmodulin complexes with brain and muscle creatine kinase peptides ', Current Research in Structural Biology, vol. 3, pp. 121-132 . https://doi.org/10.1016/j.crstbi.2021.05.001 |
| ISSN: | 2665-928X |
| DOI: | 10.1016/j.crstbi.2021.05.001 |
| Popis: | Current research in structural biology 3, 121-132 (2021). doi:10.1016/j.crstbi.2021.05.001 Calmodulin (CaM) is a ubiquitous Ca$^{2+}$ sensing protein that binds to and modulates numerous target proteins and enzymes during cellular signaling processes. A large number of CaM-target complexes have been identified and structurally characterized, revealing a wide diversity of CaM-binding modes. A newly identified target is creatine kinase (CK), a central enzyme in cellular energy homeostasis. This study reports two high-resolution X-ray structures, determined to 1.24 ����� and 1.43 ����� resolution, of calmodulin in complex with peptides from human brain and muscle CK, respectively. Both complexes adopt a rare extended binding mode with an observed stoichiometry of 1:2 CaM:peptide, confirmed by isothermal titration calorimetry, suggesting that each CaM domain independently binds one CK peptide in a Ca$^{2+}$-depended manner. While the overall binding mode is similar between the structures with muscle or brain-type CK peptides, the most significant difference is the opposite binding orientation of the peptides in the N-terminal domain. This may extrapolate into distinct binding modes and regulation of the full-length CK isoforms. The structural insights gained in this study strengthen the link between cellular energy homeostasis and Ca$^{2+}$-mediated cell signaling and may shed light on ways by which cells can ���fine tune��� their energy levels to match the spatial and temporal demands. Published by Elsevier, Amsterdam |
| Databáze: | OpenAIRE |
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