2K60
| NMR structure of calcium-loaded STIM1 EF-SAM | Descriptor: | CALCIUM ION, PROTEIN (Stromal interaction molecule 1) | Authors: | Stathopulos, P.B, Ikura, M. | Deposit date: | 2008-07-02 | Release date: | 2008-10-07 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR | Cite: | Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry. Cell(Cambridge,Mass.), 135, 2008
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2MAJ
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2MAK
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6PW7
| X-ray crystal structure of C. elegans STIM EF-SAM domain | Descriptor: | CALCIUM ION, Stromal interaction molecule 1 | Authors: | Enomoto, M, Nishikawa, T, Back, S.I, Ishiyama, N, Zheng, L, Stathopulos, P.B, Ikura, M. | Deposit date: | 2019-07-22 | Release date: | 2019-11-13 | Last modified: | 2020-02-12 | Method: | X-RAY DIFFRACTION (1.89 Å) | Cite: | Coordination of a Single Calcium Ion in the EF-hand Maintains the Off State of the Stromal Interaction Molecule Luminal Domain. J.Mol.Biol., 432, 2020
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1X9A
| Solution NMR Structure of Protein Tm0979 from Thermotoga maritima. Ontario Center for Structural Proteomics Target TM0979_1_87; Northeast Structural Genomics Consortium Target VT98. | Descriptor: | hypothetical protein TM0979 | Authors: | Gaspar, J.A, Liu, C, Vassall, K.A, Stathopulos, P.B, Meglei, G, Stephen, R, Pineda-Lucena, A, Wu, B, Yee, A, Arrowsmith, C.H, Meiering, E.M, Northeast Structural Genomics Consortium (NESG) | Deposit date: | 2004-08-20 | Release date: | 2004-12-07 | Last modified: | 2024-05-22 | Method: | SOLUTION NMR | Cite: | A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima. Protein Sci., 14, 2005
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5KUE
| Human SeMet incorporated I141M/L146M mitochondrial calcium uniporter (residues 72-189) crystal structure with magnesium | Descriptor: | 1,2-ETHANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Calcium uniporter protein, ... | Authors: | Mok, C.Y.M, Lee, S.K, Junop, M.S, Stathopulos, P.B. | Deposit date: | 2016-07-13 | Release date: | 2016-09-07 | Last modified: | 2020-01-08 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Structural Insights into Mitochondrial Calcium Uniporter Regulation by Divalent Cations. Cell Chem Biol, 23, 2016
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5KUI
| Human mitochondrial calcium uniporter (residues 72-189) crystal structure with calcium. | Descriptor: | Calcium uniporter protein, mitochondrial | Authors: | Mok, M.C.Y, Lee, S.K, Junop, M.S, Stathopulos, P.B. | Deposit date: | 2016-07-13 | Release date: | 2016-09-07 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (2.701 Å) | Cite: | Structural Insights into Mitochondrial Calcium Uniporter Regulation by Divalent Cations. Cell Chem Biol, 23, 2016
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5KUJ
| Human mitochondrial calcium uniporter (residues 72-189) crystal structure with magnesium. | Descriptor: | Calcium uniporter protein, mitochondrial, MAGNESIUM ION | Authors: | Mok, M.C.Y, Lee, S.K, Junop, M.S, Stathopulos, P.B. | Deposit date: | 2016-07-13 | Release date: | 2016-09-07 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Structural Insights into Mitochondrial Calcium Uniporter Regulation by Divalent Cations. Cell Chem Biol, 23, 2016
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5KUG
| Human mitochondrial calcium uniporter (residues 72-189) crystal structure with lithium | Descriptor: | Calcium uniporter protein, mitochondrial | Authors: | Mok, M.C.Y, Lee, S.K, Junop, M.S, Stathopulos, P.B. | Deposit date: | 2016-07-13 | Release date: | 2016-09-07 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structural Insights into Mitochondrial Calcium Uniporter Regulation by Divalent Cations. Cell Chem Biol, 23, 2016
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2L5Y
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3UJ4
| Crystal structure of the apo-inositol 1,4,5-trisphosphate receptor | Descriptor: | Inositol 1,4,5-trisphosphate receptor type 1, SULFATE ION | Authors: | Ikura, M, Seo, M.D, Ishiyama, N, Stathopulos, P. | Deposit date: | 2011-11-07 | Release date: | 2012-02-15 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (3 Å) | Cite: | Structural and functional conservation of key domains in InsP3 and ryanodine receptors. Nature, 483, 2012
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3UJ0
| Crystal structure of the inositol 1,4,5-trisphosphate receptor with ligand bound form. | Descriptor: | D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE, Inositol 1,4,5-trisphosphate receptor type 1 | Authors: | Ikura, M, Seo, M.D, Ishiyama, N, Stathopulos, P. | Deposit date: | 2011-11-07 | Release date: | 2012-02-15 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (3.6 Å) | Cite: | Structural and functional conservation of key domains in InsP3 and ryanodine receptors. Nature, 483, 2012
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2MC2
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4KEJ
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4KEK
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4KEI
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2MSD
| NMR data-driven model of GTPase KRas-GNP tethered to a lipid-bilayer nanodisc | Descriptor: | 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, Apolipoprotein A-I, GTPase KRas, ... | Authors: | Mazhab-Jafari, M, Stathopoulos, P, Marshall, C, Ikura, M. | Deposit date: | 2014-07-29 | Release date: | 2015-06-03 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR | Cite: | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc.Natl.Acad.Sci.USA, 112, 2015
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2MSE
| NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc | Descriptor: | 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, Apolipoprotein A-I, GTPase KRas, ... | Authors: | Mazhab-Jafari, M, Stathopoulos, P, Marshall, C, Ikura, M. | Deposit date: | 2014-07-29 | Release date: | 2015-06-03 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR | Cite: | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc.Natl.Acad.Sci.USA, 112, 2015
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2MSC
| NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc | Descriptor: | 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, Apolipoprotein A-I, GTPase KRas, ... | Authors: | Mazhab-Jafari, M, Stathopoulos, P, Marshall, C, Ikura, M. | Deposit date: | 2014-07-29 | Release date: | 2015-06-03 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR | Cite: | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc.Natl.Acad.Sci.USA, 112, 2015
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