Genomes and Genes
Affiliation: Harvard University
- Structural characterization of the RyR1-FKBP12 interactionMontserrat Samso
Brigham and Women s Hospital, Harvard Medical School, Boston, MA 02115, USA
J Mol Biol 356:917-27. 2006..The orientation of RyR1-bound FKBP12, with part of its FK506 binding site facing towards RyR1, allows us to propose how FK506 is involved in the dissociation of FKBP12 from RyR1...
- Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EMMontserrat Samso
Brigham and Women s Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA
Nat Struct Mol Biol 12:539-44. 2005..The resulting constricted axial structure provides direct continuity between cytoplasmic and transmembrane assemblies, and a possible mechanism for control of channel gating through conformational changes in the cytoplasmic assembly...
- Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gatingMontserrat Samso
Division of Anesthesia Research, Department of Anesthesia, Perioperative and Pain Medicine, Brigham and Women s Hospital, Harvard Medical School, Boston, Massachusetts, USA
PLoS Biol 7:e85. 2009....
- 3D Mapping of the SPRY2 domain of ryanodine receptor 1 by single-particle cryo-EMAlex Perálvarez-Marín
Department of Anesthesia, Brigham and Women s Hospital, Harvard Medical School, Boston, Massachusetts, United States of America
PLoS ONE 6:e25813. 2011..We report here the first 3D localization of a SPRY2 domain in any known RyR isoform...
- Three-dimensional localization of the α and β subunits and of the II-III loop in the skeletal muscle L-type Ca2+ channelJohn Szpyt
Department of Anesthesia, Brigham and Women s Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA
J Biol Chem 287:43853-61. 2012..The β subunit appears more closely associated to the membrane than expected, which may better account for both its role in localizing the α(1s) subunit to the membrane and its suggested role in excitation-contraction coupling...