Structural and dynamic insights into the subtype-specific IP3-binding mechanism of the IP3 receptor
| العنوان: | Structural and dynamic insights into the subtype-specific IP3-binding mechanism of the IP3 receptor |
|---|---|
| المؤلفون: | Su Youn Lee, Min-Duk Seo, Hee-Seop Yoo, Ka Young Chung, Hye-Seung Choi |
| المصدر: | The Biochemical journal. 473(20) |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Circular dichroism, IP3 binding, Release channel, Inositol 1,4,5-Trisphosphate, Bioinformatics, Endoplasmic Reticulum, Biochemistry, Models, Biological, Mass Spectrometry, Cell Line, 03 medical and health sciences, chemistry.chemical_compound, Mice, Escherichia coli, Animals, Humans, Inositol 1,4,5-Trisphosphate Receptors, Inositol, Receptor, Molecular Biology, 030102 biochemistry & molecular biology, Mechanism (biology), Isothermal titration calorimetry, Cell Biology, Inositol trisphosphate receptor, 030104 developmental biology, chemistry, Biophysics, Thermodynamics, Calcium Channels, Signal Transduction |
| الوصف: | There are three subtypes of vertebrate inositol 1,4,5-trisphosphate receptor (IP 3 R), a Ca 2+ -release channel on the ER membrane-IP 3 R1, IP 3 R2, and IP 3 R3-each of which has a distinctive role in disease development. To determine the subtype-specific IP 3 -binding mechanism, we compared the thermodynamics, thermal stability, and conformational dynamics between the N-terminal regions of IP 3 R1 (IP 3 R1-NT) and IP 3 R3 (IP 3 R3-NT) by performing circular dichroism (CD), isothermal titration calorimetry (ITC), and hydrogen-deuterium exchange mass spectrometry (HDX-MS). Previously determined crystal structures of IP 3 R1-NT and HDX-MS results from this study revealed that both IP 3 R1 and IP 3 R3 adopt a similar IP 3 -binding mechanism. However, several regions, including the α- and β-interfaces, of IP 3 R1-NT and IP 3 R3-NT show significantly different conformational dynamics upon IP 3 binding, which may explain the different IP 3 -binding affinities between the subtypes. The importance of the interfaces for subtype-specific IP 3 binding is also supported by the different dynamic conformations of the two subtypes in the apo-states. Furthermore, IP 3 R1-NT and IP 3 R3-NT show different IP 3 -binding affinities and thermal stabilities, but share similar thermodynamic properties for IP 3 binding. These results collectively provide new insights into the mechanism underlying IP 3 binding to IP 3 Rs and the subtype-specific regulatory mechanism. |
| تدمد: | 1470-8728 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afbc235d634953ab726912c3e28e2e7bTest https://pubmed.ncbi.nlm.nih.gov/27444647Test |
| رقم الانضمام: | edsair.doi.dedup.....afbc235d634953ab726912c3e28e2e7b |
| قاعدة البيانات: | OpenAIRE |
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