Download MendeleyCrystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex.
Schumacher, M.A., Crum, M., Miller, M.C.(2004) Structure 12: 849-860
- PubMed: 15130477
- DOI: https://doi.org/10.1016/j.str.2004.03.017
- Primary Citation of Related Structures:
1QX5, 1QX7 - PubMed Abstract:
Small conductance Ca2+-activated K+ channels (SK channels) are composed of the pore-forming alpha subunit and calmodulin (CaM). CaM binds to a region of the alpha subunit called the CaM binding domain (CaMBD), located intracellular and immediately C-terminal to the inner helix gate, in either the presence or absence of Ca2+. SK gating occurs when Ca2+ binds the N lobe of CaM thereby transmitting the signal to the attached inner helix gate to open. Here we present crystal structures of apoCaM and apoCaM/SK2 CaMBD complex. Several apoCaM crystal forms with multiple (12) packing environments reveal the same EF hand domain-swapped dimer providing potentially new insight into CaM regulation. The apoCaM/SK2 CaMBD structure, combined with our Ca2+/CaM/CaMBD structure suggests that Ca2+ binding induces folding and dimerization of the CaMBD, which causes large CaMBD-CaM C lobe conformational changes, including a >90 degrees rotation of the region of the CaMBD directly connected to the gate.
Organizational Affiliation:
Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, OR 97239 USA. [email protected]
