5TP6

Solution structure of the CaM34 with the iNOS CaM binding domain peptide

5TP6 の概要

• エントリーDOI: 10.2210/pdb5tp6/pdb
• 関連するPDBエントリー: 5TP5
• NMR情報: BMRB: 30196
• 分子名称: Calmodulin, Nitric oxide synthase, inducible (2 entities in total)
• 機能のキーワード: calcium deficient, nitric oxide synthase, oxidoreductase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20035.70

構造登録者

Piazza, M.,Dieckmann, T.,Guillemette, J.G. (登録日: 2016-10-19, 公開日: 2017-09-27, 最終更新日: 2024-05-01)

主引用文献

Piazza, M.,Taiakina, V.,Dieckmann, T.,Guillemette, J.G.
Structural Consequences of Calmodulin EF Hand Mutations.
Biochemistry, 56:944-956, 2017

PubMed Abstract: Calmodulin (CaM) is a cytosolic Ca-binding protein that serves as a control element for many enzymes. It consists of two globular domains, each containing two EF hand pairs capable of binding Ca, joined by a flexible central linker region. CaM is able to bind and activate its target proteins in the Ca-replete and Ca-deplete forms. To study the Ca-dependent/independent properties of binding and activation of target proteins by CaM, CaM constructs with Ca-binding disrupting mutations of Asp to Ala at position one of each EF hand have been used. These CaM mutant proteins are deficient in binding Ca in either the N-lobe EF hands (CaM), C-lobe EF hands (CaM), or all four EF hands (CaM). To investigate potential structural changes these mutations may cause, we performed detailed NMR studies of CaM, CaM, and CaM including determining the solution structure of CaM. We then investigated if these CaM mutants affected the interaction of CaM with a target protein known to interact with apoCaM by determining the solution structure of CaM bound to the iNOS CaM binding domain peptide. The structures provide direct structural evidence of changes that are present in these Ca-deficient CaM mutants and show these mutations increase the hydrophobic exposed surface and decrease the electronegative surface potential throughout each lobe of CaM. These Ca-deficient CaM mutants may not be a true representation of apoCaM and may not allow for native-like interactions of apoCaM with its target proteins.

PubMed: 28121131
DOI: 10.1021/acs.biochem.6b01296

実験手法

SOLUTION NMR