1PIN
| PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS | Descriptor: | 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, ALANINE, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, ... | Authors: | Noel, J.P, Ranganathan, R, Hunter, T. | Deposit date: | 1998-06-21 | Release date: | 1998-10-14 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (1.35 Å) | Cite: | Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell(Cambridge,Mass.), 89, 1997
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1F8A
| STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS | Descriptor: | PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, Y(SEP)PT(SEP)S PEPTIDE | Authors: | Verdecia, M.A, Bowman, M.E, Lu, K.P, Hunter, T, Noel, J.P. | Deposit date: | 2000-06-29 | Release date: | 2000-08-23 | Last modified: | 2013-05-22 | Method: | X-RAY DIFFRACTION (1.84 Å) | Cite: | Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat.Struct.Biol., 7, 2000
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1J6Y
| Solution structure of Pin1At from Arabidopsis thaliana | Descriptor: | peptidyl-prolyl cis-trans isomerase | Authors: | Landrieu, I, Wieruszeski, J.M, Wintjens, R, Inze, D, Lippens, G. | Deposit date: | 2001-05-15 | Release date: | 2002-08-07 | Last modified: | 2024-05-22 | Method: | SOLUTION NMR | Cite: | Solution Structure of the
Single-domain Prolyl Cis/Trans
Isomerase PIN1At from Arabidopsis thaliana J.Mol.Biol., 320, 2002
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1M5Y
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1NMV
| Solution structure of human Pin1 | Descriptor: | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | Authors: | Bayer, E, Goettsch, S, Mueller, J.W, Griewel, B, Guiberman, E, Mayr, L, Bayer, P. | Deposit date: | 2003-01-11 | Release date: | 2003-08-12 | Last modified: | 2024-05-22 | Method: | SOLUTION NMR | Cite: | Structural Analysis of the Mitotic Regulator hPin1 in Solution: INSIGHTS INTO DOMAIN ARCHITECTURE AND SUBSTRATE BINDING. J.Biol.Chem., 278, 2003
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1NMW
| Solution structure of the PPIase domain of human Pin1 | Descriptor: | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, SULFATE ION | Authors: | Bayer, E, Goettsch, S, Mueller, J.W, Griewel, B, Guiberman, E, Mayr, L, Bayer, P. | Deposit date: | 2003-01-12 | Release date: | 2003-07-15 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR | Cite: | Structural Analysis of the Mitotic Regulator hPin1 in Solution: INSIGHTS INTO DOMAIN ARCHITECTURE AND SUBSTRATE BINDING. J.Biol.Chem., 278, 2003
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1YW5
| Peptidyl-prolyl isomerase ESS1 from Candida albicans | Descriptor: | peptidyl prolyl cis/trans isomerase | Authors: | Li, Z, Li, H, Devasahayam, G, Gemmill, T, Chaturvedi, V, Hanes, S.D, Van Roey, P. | Deposit date: | 2005-02-17 | Release date: | 2005-04-26 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | The Structure of the Candida albicans Ess1 Prolyl Isomerase Reveals a Well-Ordered Linker that Restricts Domain Mobility Biochemistry, 44, 2005
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1ZCN
| human Pin1 Ng mutant | Descriptor: | PENTAETHYLENE GLYCOL, PHOSPHATE ION, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | Authors: | Jager, M, Zhang, Y, Nguyen, H, Dendel, G, Bowman, M.E, Gruebele, M, Noel, J.P, Kelly, J.W. | Deposit date: | 2005-04-12 | Release date: | 2006-06-20 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structure-function-folding relationship in a WW domain. Proc.Natl.Acad.Sci.Usa, 103, 2006
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2F21
| human Pin1 Fip mutant | Descriptor: | PENTAETHYLENE GLYCOL, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | Authors: | Jager, M, Zhang, Y, Bowman, M.E, Noel, J.P, Kelly, J.W. | Deposit date: | 2005-11-15 | Release date: | 2006-06-20 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Structure-function-folding relationship in a WW domain. Proc.Natl.Acad.Sci.Usa, 103, 2006
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2ITK
| human Pin1 bound to D-PEPTIDE | Descriptor: | 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, D-Peptide, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | Authors: | Noel, J.P, Zhang, Y. | Deposit date: | 2006-10-19 | Release date: | 2007-05-22 | Last modified: | 2023-11-15 | Method: | X-RAY DIFFRACTION (1.45 Å) | Cite: | Structural basis for high-affinity peptide inhibition of human Pin1. Acs Chem.Biol., 2, 2007
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2PV2
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2PV1
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2PV3
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2Q5A
| human Pin1 bound to L-PEPTIDE | Descriptor: | 3,6,9,12,15,18-HEXAOXAICOSANE, Five residue peptide, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | Authors: | Noel, J.P, Zhang, Y. | Deposit date: | 2007-05-31 | Release date: | 2007-06-26 | Last modified: | 2011-07-13 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Structural basis for high-affinity peptide inhibition of human Pin1. Acs Chem.Biol., 2, 2007
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2JZV
| Solution structure of S. aureus PrsA-PPIase | Descriptor: | Foldase protein prsA | Authors: | Seppala, R, Tossavainen, H, Heikkinen, S, Koskela, H, Kontinen, V, Permi, P. | Deposit date: | 2008-01-21 | Release date: | 2009-01-20 | Last modified: | 2024-05-29 | Method: | SOLUTION NMR | Cite: | Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA - Implications for the catalytic mechanism of parvulins. Bmc Struct.Biol., 9, 2009
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2ZQU
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2ZQS
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2ZQT
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2ZQV
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2ZR4
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2ZR5
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2ZR6
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3GPK
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3I6C
| Structure-Based Design of Novel PIN1 Inhibitors (II) | Descriptor: | 3-fluoro-N-(naphthalen-2-ylcarbonyl)-D-phenylalanine, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | Authors: | Greasley, S.E, Ferre, R.A. | Deposit date: | 2009-07-06 | Release date: | 2010-04-21 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (1.3 Å) | Cite: | Structure-based design of novel human Pin1 inhibitors (II). Bioorg.Med.Chem.Lett., 20, 2010
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3IKD
| Structure-Based Design of Novel PIN1 Inhibitors (I) | Descriptor: | (2R)-2-[(1-benzothiophen-2-ylcarbonyl)amino]-3-phenylpropyl phosphate, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | Authors: | Matthews, D, Greasley, S, Ferre, R, Parge, H. | Deposit date: | 2009-08-05 | Release date: | 2009-09-22 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure-based design of novel human Pin1 inhibitors (I). Bioorg.Med.Chem.Lett., 19, 2009
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