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6R2W
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BU of 6r2w by Molmil
Crystal structure of the super-active FVIIa variant VYT in complex with tissue factor
分子名称: CALCIUM ION, Coagulation factor VII, N-acetyl-D-phenylalanyl-N-[(2S,3S)-6-carbamimidamido-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide, ...
著者Sorensen, A.B, Svensson, L.A, Gandhi, P.S.
登録日2019-03-19
公開日2019-12-11
最終更新日2024-01-24
実験手法X-RAY DIFFRACTION (1.25 Å)
主引用文献Beating tissue factor at its own game: Design and properties of a soluble tissue factor-independent coagulation factor VIIa.
J.Biol.Chem., 295, 2020
4Z6A
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BU of 4z6a by Molmil
Crystal Structure of a FVIIa-Trypsin Chimera (YT) in Complex with Soluble Tissue Factor
分子名称: CALCIUM ION, CITRIC ACID, Coagulation factor VII, ...
著者Sorensen, A.B, Svensson, L.A, Gandhi, P.S.
登録日2015-04-04
公開日2015-12-30
最終更新日2024-01-10
実験手法X-RAY DIFFRACTION (2.25 Å)
主引用文献Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity.
J.Biol.Chem., 291, 2016
4ZMA
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BU of 4zma by Molmil
Crystal Structure of a FVIIa-Trypsin Chimera (ST) in Complex with Soluble Tissue Factor
分子名称: CACODYLATE ION, CALCIUM ION, Coagulation factor VII, ...
著者Sorensen, A.B, Svensson, L.A, Gandhi, P.S.
登録日2015-05-02
公開日2015-12-30
最終更新日2024-01-10
実験手法X-RAY DIFFRACTION (2.3 Å)
主引用文献Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity.
J.Biol.Chem., 291, 2016
4YLQ
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BU of 4ylq by Molmil
Crystal Structure of a FVIIa-Trypsin Chimera (FT) in Complex with Soluble Tissue Factor
分子名称: CALCIUM ION, Coagulation factor VII, N-PROPANOL, ...
著者Sorensen, A.B, Svensson, L.A, Gandhi, P.S.
登録日2015-03-05
公開日2015-12-30
最終更新日2024-01-10
実験手法X-RAY DIFFRACTION (1.4 Å)
主引用文献Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity.
J.Biol.Chem., 291, 2016
6Y94
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BU of 6y94 by Molmil
Ca2+-bound Calmodulin mutant N53I
分子名称: CALCIUM ION, Calmodulin
著者Holt, C, Nielsen, L.H, Lau, K, Brohus, M, Sorensen, A.B, Larsen, K.T, Sommer, C, Petegem, F.V, Overgaard, M.T, Wimmer, R.
登録日2020-03-06
公開日2020-04-29
最終更新日2024-06-19
実験手法SOLUTION NMR
主引用文献The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-terminal domain, altering its interaction with the cardiac ryanodine receptor.
J.Biol.Chem., 295, 2020
6Y4P
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BU of 6y4p by Molmil
Calmodulin N53I variant bound to cardiac ryanodine receptor (RyR2) calmodulin binding domain
分子名称: CALCIUM ION, Calmodulin-1, Ryanodine receptor 2
著者Lau, K, Nielsen, L.H, Holt, C, Brohus, M, Sorensen, A.B, Larsen, K.T, Sommer, C, Van Petegem, F, Overgaard, M.T, Wimmer, R.
登録日2020-02-21
公開日2020-04-29
最終更新日2024-01-24
実験手法X-RAY DIFFRACTION (2.13325572 Å)
主引用文献The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-terminal domain, altering its interaction with the cardiac ryanodine receptor.
J.Biol.Chem., 295, 2020
6Y4O
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BU of 6y4o by Molmil
Calmodulin bound to cardiac ryanodine receptor (RyR2) calmodulin binding domain
分子名称: CALCIUM ION, Calmodulin-2, Ryanodine receptor 2
著者Lau, K, Nielsen, L.H, Holt, C, Brohus, M, Sorensen, A.B, Larsen, K.T, Sommer, C, Van Petegem, F, Overgaard, M.T, Wimmer, R.
登録日2020-02-21
公開日2020-04-29
最終更新日2024-01-24
実験手法X-RAY DIFFRACTION (1.83549082 Å)
主引用文献The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-terminal domain, altering its interaction with the cardiac ryanodine receptor.
J.Biol.Chem., 295, 2020
6Y95
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BU of 6y95 by Molmil
Ca2+-free Calmodulin mutant N53I
分子名称: Calmodulin
著者Holt, C, Hamborg, L.N, Lau, K, Brohus, M, Sorensen, A.B, Larsen, K.T, Sommer, C, Petegem, F.V, Overgaard, M.T, Wimmer, R.
登録日2020-03-06
公開日2020-04-29
最終更新日2024-06-19
実験手法SOLUTION NMR
主引用文献The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-terminal domain, altering its interaction with the cardiac ryanodine receptor.
J.Biol.Chem., 295, 2020

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件を2024-11-06に公開中

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