7BF1
Ca2+-Calmodulin in complex with peptide from brain-type creatine kinase in extended 1:2 binding mode
これはPDB形式変換不可エントリーです。
7BF1 の概要
エントリーDOI | 10.2210/pdb7bf1/pdb |
分子名称 | Calmodulin-1, Creatine kinase B-type, CALCIUM ION, ... (5 entities in total) |
機能のキーワード | calmodulin, calmodulin-peptide complex, creatine kinase, calcium signaling, energy metabolism, cytosolic protein |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 21460.14 |
構造登録者 | Sprenger, J.,Akerfeldt, K.S.,Bredfelt, J.,Patel, N.,Rowlett, R.,Trifan, A.,Vanderbeck, A.,Lo Leggio, L.,Snogerup Linse, S. (登録日: 2020-12-31, 公開日: 2021-07-21, 最終更新日: 2024-01-31) |
主引用文献 | Sprenger, J.,Trifan, A.,Patel, N.,Vanderbeck, A.,Bredfelt, J.,Tajkhorshid, E.,Rowlett, R.,Lo Leggio, L.,Akerfeldt, K.S.,Linse, S. Calmodulin complexes with brain and muscle creatine kinase peptides. Curr Res Struct Biol, 3:121-132, 2021 Cited by PubMed Abstract: Calmodulin (CaM) is a ubiquitous Ca 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 Å and 1.43 Å 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-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-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. PubMed: 34235492DOI: 10.1016/j.crstbi.2021.05.001 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.24 Å) |
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