%0 Journal Article %1 Sery_2005_427 %A Serysheva, Irina I %A Hamilton, Susan L %A Chiu, Wah %A Ludtke, Steven J %D 2005 %J J. Mol. Biol. %K Algorithms; Calcium Channel Conformation; Models, Molecular; Protein Receptor Release Ryanodine %N 3 %P 427--431 %R 10.1016/j.jmb.2004.10.073 %T Structure of Ca$^2+$ release channel at 14 A resolution. %U http://dx.doi.org/10.1016/j.jmb.2004.10.073 %V 345 %X The 14 A resolution structure of the 2.3 MDa Ca$^2+$ release channel (also known as RyR1) was determined by electron cryomicroscopy and single particle reconstruction. This structure was produced using collected data used for our previous published structures at 22-30 A resolution, but now taking advantage of recent algorithmic improvements in the EMAN software suite. This improved map clearly exhibits more structural detail and allows better defined docking of computationally predicted structural domain folds. Using sequence-based fold recognition, the N-terminal region of RyR1, residues 216-572, was predicted to have significant structural similarity with the IP3-binding core region of the type 1 IP3R. This putative structure was computationally localized to the clamp-shaped region of RyR1, which has been implicated to have a regulatory role in the channel activity.

@article{Sery_2005_427, abstract = {The 14 A resolution structure of the 2.3 MDa {C}a$^{2+}$ release channel (also known as RyR1) was determined by electron cryomicroscopy and single particle reconstruction. This structure was produced using collected data used for our previous published structures at 22-30 A resolution, but now taking advantage of recent algorithmic improvements in the EMAN software suite. This improved map clearly exhibits more structural detail and allows better defined docking of computationally predicted structural domain folds. Using sequence-based fold recognition, the N-terminal region of RyR1, residues 216-572, was predicted to have significant structural similarity with the IP3-binding core region of the type 1 IP3R. This putative structure was computationally localized to the clamp-shaped region of RyR1, which has been implicated to have a regulatory role in the channel activity.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Serysheva, Irina I and Hamilton, Susan L and Chiu, Wah and Ludtke, Steven J}, biburl = {https://www.bibsonomy.org/bibtex/29b1e42d973445aec09782e4d9fd82733/hake}, description = {The whole bibliography file I use.}, doi = {10.1016/j.jmb.2004.10.073}, file = {Sery_2005_427.pdf:Sery_2005_427.pdf:PDF}, interhash = {65574ad089eea88bbe5e8dadcb80d251}, intrahash = {9b1e42d973445aec09782e4d9fd82733}, journal = {J. Mol. Biol.}, keywords = {Algorithms; Calcium Channel Conformation; Models, Molecular; Protein Receptor Release Ryanodine}, month = Jan, number = 3, pages = {427--431}, pii = {S0022-2836(04)01379-8}, pmid = {15581887}, timestamp = {2009-06-03T11:21:29.000+0200}, title = {Structure of {C}a$^{2+}$ release channel at 14 A resolution.}, url = {http://dx.doi.org/10.1016/j.jmb.2004.10.073}, volume = 345, year = 2005 }