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1CNP
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BU of 1cnp by Molmil
THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES
分子名称: CALCYCLIN (RABBIT, APO)
著者Potts, B.C.M, Smith, J, Akke, M, Macke, T.J, Okazaki, K, Hidaka, H, Case, D.A, Chazin, W.J.
登録日1995-08-31
公開日1996-10-14
最終更新日2024-05-22
実験手法SOLUTION NMR
主引用文献The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.
Nat.Struct.Biol., 2, 1995
2CNP
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BU of 2cnp by Molmil
HIGH RESOLUTION SOLUTION STRUCTURE OF APO RABBIT CALCYCLIN, NMR, 22 STRUCTURES
分子名称: CALCYCLIN
著者Maler, L, Potts, B.C.M, Chazin, W.J.
登録日1999-01-07
公開日1999-07-22
最終更新日2024-05-22
実験手法SOLUTION NMR
主引用文献High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins.
J.Biomol.NMR, 13, 1999
3HYE
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BU of 3hye by Molmil
Crystal structure of 20S proteasome in complex with hydroxylated salinosporamide
分子名称: (2R,3S,4R)-2-[(S)-(1S)-cyclohex-2-en-1-yl(hydroxy)methyl]-3-hydroxy-4-(2-hydroxyethyl)-3-methyl-5-oxopyrrolidine-2-carbaldehyde, Proteasome component C1, Proteasome component C11, ...
著者Groll, M, Arthur, K.A.M, Macherla, V.R, Manam, R.R, Potts, B.C.
登録日2009-06-22
公開日2009-09-15
最終更新日2023-09-06
実験手法X-RAY DIFFRACTION (2.5 Å)
主引用文献Snapshots of the fluorosalinosporamide/20S complex offer mechanistic insights for fine tuning proteasome inhibition
J.Med.Chem., 52, 2009
2FAK
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BU of 2fak by Molmil
Crystal structure of Salinosporamide A in complex with the yeast 20S proteasome
分子名称: (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE, Proteasome component C1, Proteasome component C11, ...
著者Groll, M, Potts, B.C.
登録日2005-12-07
公開日2006-04-18
最終更新日2023-05-31
実験手法X-RAY DIFFRACTION (2.8 Å)
主引用文献Crystal Structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in Complex with the 20S Proteasome Reveal Important Consequences of beta-Lactone Ring Opening and a Mechanism for Irreversible Binding.
J.Am.Chem.Soc., 128, 2006
1A03
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BU of 1a03 by Molmil
THE THREE-DIMENSIONAL STRUCTURE OF CA2+-BOUND CALCYCLIN: IMPLICATIONS FOR CA2+-SIGNAL TRANSDUCTION BY S100 PROTEINS, NMR, 20 STRUCTURES
分子名称: CALCYCLIN (RABBIT, CA2+)
著者Sastry, M, Ketchem, R.R, Crescenzi, O, Weber, C, Lubienski, M.J, Hidaka, H, Chazin, W.J.
登録日1997-12-08
公開日1999-03-02
最終更新日2024-05-22
実験手法SOLUTION NMR
主引用文献The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins.
Structure, 6, 1998
3GPW
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BU of 3gpw by Molmil
Crystal structure of the yeast 20S proteasome in complex with Salinosporamide derivatives: irreversible inhibitor ligand
分子名称: (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE, Proteasome component C1, Proteasome component C11, ...
著者Groll, M, Macherla, V.R, Manam, R.R, Arthur, K.A.M, Potts, C.B.
登録日2009-03-23
公開日2009-09-15
最終更新日2023-09-20
実験手法X-RAY DIFFRACTION (2.5 Å)
主引用文献Snapshots of the fluorosalinosporamide/20S complex offer mechanistic insights for fine tuning proteasome inhibition
J.Med.Chem., 52, 2009
3GPT
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BU of 3gpt by Molmil
Crystal structure of the yeast 20S proteasome in complex with Salinosporamide derivatives: slow substrate ligand
分子名称: (2R,3S,4R)-2-[(S)-(1S)-cyclohex-2-en-1-yl(hydroxy)methyl]-4-(2-fluoroethyl)-3-hydroxy-3-methyl-5-oxopyrrolidine-2-carbaldehyde, Proteasome component C1, Proteasome component C11, ...
著者Groll, M, Macherla, V.R, Manam, R.R, Arthur, K.A.M, Potts, C.B.
登録日2009-03-23
公開日2009-09-15
最終更新日2023-09-06
実験手法X-RAY DIFFRACTION (2.41 Å)
主引用文献Snapshots of the fluorosalinosporamide/20S complex offer mechanistic insights for fine tuning proteasome inhibition
J.Med.Chem., 52, 2009
1JWD
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BU of 1jwd by Molmil
Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.
分子名称: Calcyclin
著者Maler, L, Sastry, M, Chazin, W.J.
登録日2001-09-04
公開日2002-03-27
最終更新日2024-05-22
実験手法SOLUTION NMR
主引用文献A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin
J.Mol.Biol., 317, 2002

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