دورية أكاديمية
Structural, Biochemical, and Functional Characterization of the Cyclic Nucleotide Binding Homology Domain from the Mouse EAG1 Potassium Channel.
| العنوان: | Structural, Biochemical, and Functional Characterization of the Cyclic Nucleotide Binding Homology Domain from the Mouse EAG1 Potassium Channel. |
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| المؤلفون: | Marques-Carvalho, Maria J, Sahoo, Nirakar, Muskett, Frederick W, Vieira-Pires, Ricardo S, Gabant, Guillaume, Cadene, Martine, Schönherr, Roland, Morais-Cabral, João H |
| المساهمون: | Instituto de Biologia Molecular e Celular (IBMC), Jena University Hospital Jena, University of Leicester, Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto = University of Porto, Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Université de Tours (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | ISSN: 0022-2836. |
| بيانات النشر: | HAL CCSD Elsevier |
| سنة النشر: | 2012 |
| المجموعة: | Université François-Rabelais de Tours: HAL |
| مصطلحات موضوعية: | [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology |
| الوصف: | International audience ; KCNH channels are voltage-gated potassium channels with important physiological functions. In these channels, a C-terminal cytoplasmic region, known as the cyclic nucleotide binding homology (CNB-homology) domain displays strong sequence similarity to cyclic nucleotide binding (CNB) domains. However, the isolated domain does not bind cyclic nucleotides. Here, we report the X-ray structure of the CNB-homology domain from the mouse EAG1 channel. Through comparison with the recently determined structure of the CNB-homology domain from the zebrafish ELK (eag-like K(+)) channel and the CNB domains from the MlotiK1 and HCN (hyperpolarization-activated cyclic nucleotide-gated) potassium channels, we establish the structural features of CNB-homology domains that explain the low affinity for cyclic nucleotides. Our structure establishes that the "self-liganded" conformation, where two residues of the C-terminus of the domain are bound in an equivalent position to cyclic nucleotides in CNB domains, is a conserved feature of CNB-homology domains. Importantly, we provide biochemical evidence that suggests that there is also an unliganded conformation where the C-terminus of the domain peels away from its bound position. A functional characterization of this unliganded conformation reveals a role of the CNB-homology domain in channel gating. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/22732247; hal-00747621; https://hal.science/hal-00747621Test; PUBMED: 22732247 |
| DOI: | 10.1016/j.jmb.2012.06.025 |
| الإتاحة: | https://doi.org/10.1016/j.jmb.2012.06.025Test https://hal.science/hal-00747621Test |
| رقم الانضمام: | edsbas.471D3046 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.jmb.2012.06.025 |
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