4Q5U

Structure of calmodulin bound to its recognition site from calcineurin

4Q5U の概要

• エントリーDOI: 10.2210/pdb4q5u/pdb
• 分子名称: Calmodulin, Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: ef hand, calcium binding protein-protein binding complex, calcium binding protein/protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle: P62158; Cell membrane (By similarity): Q08209
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19833.35

構造登録者

Guo, H.,Dunlap, T.B.,Creamer, T.P.,Vander Kooi, C.W. (登録日: 2014-04-17, 公開日: 2014-09-03, 最終更新日: 2023-09-20)

主引用文献

Dunlap, T.B.,Guo, H.F.,Cook, E.C.,Holbrook, E.,Rumi-Masante, J.,Lester, T.E.,Colbert, C.L.,Vander Kooi, C.W.,Creamer, T.P.
Stoichiometry of the calcineurin regulatory domain-calmodulin complex.
Biochemistry, 53:5779-5790, 2014

PubMed Abstract: Calcineurin is an essential serine/threonine phosphatase that plays vital roles in neuronal development and function, heart growth, and immune system activation. Calcineurin is unique in that it is the only phosphatase known to be activated by calmodulin in response to increasing intracellular calcium concentrations. Calcium-loaded calmodulin binds to the regulatory domain of calcineurin, resulting in a conformational change that removes an autoinhibitory domain from the active site of the phosphatase. We have determined a 1.95 Å crystal structure of calmodulin bound to a peptide corresponding to its binding region from calcineurin. In contrast to previous structures of this complex, our structure has a stoichiometry of 1:1 and has the canonical collapsed, wraparound conformation observed for many calmodulin-substrate complexes. In addition, we have used size-exclusion chromatography and time-resolved fluorescence to probe the stoichiometry of binding of calmodulin to a construct corresponding to almost the entire regulatory domain from calcineurin, again finding a 1:1 complex. Taken in sum, our data strongly suggest that a single calmodulin protein is necessary and sufficient to bind to and activate each calcineurin enzyme.

PubMed: 25144868
DOI: 10.1021/bi5004734

実験手法

X-RAY DIFFRACTION (1.95 Å)