PDB keyword search results

1EQ3
NMR STRUCTURE OF HUMAN PARVULIN HPAR14
Descriptor:PEPTIDYL-PROLYL CIS/TRANS ISOMERASE (PPIASE)
Authors:Sekerina, E., Rahfeld, U.J., Muller, J., Fischer, G., Bayer, P.
Deposit date:2000-04-02
Release date:2001-04-04
Modification date:2009-02-24
Cite:NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
J.Mol.Biol., 301, 2000
1F8A
STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS
Descriptor:PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1 (E.C. 5.2.1.8)
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
Modification date:2013-05-22
Cite:Structural basis for phosphoserine-proline recognition by group IV WW domains.
Nat.Struct.Biol., 7, 2000
1FJD
HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14
Descriptor:PEPTIDYL PROLYL CIS/TRANS ISOMERASE
Authors:Terada, T., Shirouzu, M., Fukumori, Y., Fujimori, F., Ito, Y., Kigawa, T., Yokoyama, S., Uchida, T., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Deposit date:2000-08-08
Release date:2001-08-08
Modification date:2009-02-24
Cite:Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14.
J.Mol.Biol., 305, 2001
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
Modification date:2009-06-09
Cite:Solution Structure of the Single-domain Prolyl Cis/Trans Isomerase PIN1At from Arabidopsis thaliana
J.Mol.Biol., 320, 2002
1JNS
NMR STRUCTURE OF THE E. COLI PEPTIDYL-PROLYL CIS/TRANS-ISOMERASE PARVULIN 10
Descriptor:PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C (E.C.5.2.1.8)
Authors:Kuehlewein, A., Voll, G., Schelbert, B., Kessler, H., Fischer, G., Rahfeld, J.U., Gemmecker, G.
Deposit date:2001-07-25
Release date:2003-06-17
Modification date:2009-02-24
Cite:Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases.
Protein Sci., 13, 2004
1JNT
NMR STRUCTURE OF THE E. COLI PEPTIDYL-PROLYL CIS/TRANS-ISOMERASE PARVULIN 10
Descriptor:PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C (E.C.5.2.1.8)
Authors:Kuehlewein, A., Voll, G., Schelbert, B., Kessler, H., Fischer, G., Rahfeld, J.U., Gemmecker, G.
Deposit date:2001-07-25
Release date:2003-06-17
Modification date:2009-02-24
Cite:Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases.
Protein Sci., 13, 2004
1M5Y
CRYSTALLOGRAPHIC STRUCTURE OF SURA, A MOLECULAR CHAPERONE THAT FACILITATES OUTER MEMBRANE PORIN FOLDING
Descriptor:survival protein surA (E.C.5.2.1.8)
Authors:Bitto, E., McKay, D.B.
Deposit date:2002-07-10
Release date:2002-11-08
Modification date:2009-02-24
Cite:Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Folding of Outer Membrane Porins
Structure, 10, 2002
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
Modification date:2009-02-24
Cite:Structural Analysis of the Mitotic Regulator hPin1 in Solution: INSIGHTS INTO DOMAIN ARCHITECTURE AND SUBSTRATE BINDING.
J.Biol.Chem., 278, 2003
1NMW
SOLUTION STRUCTURE OF THE PPIASE DOMAIN 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:2003-01-12
Release date:2003-07-15
Modification date:2011-03-09
Cite:Structural Analysis of the Mitotic Regulator hPin1 in Solution: INSIGHTS INTO DOMAIN ARCHITECTURE AND SUBSTRATE BINDING.
J.Biol.Chem., 278, 2003
1PIN
PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
Descriptor:PEPTIDYL-PROLYL CIS-TRANS ISOMERASE (E.C.5.2.1.8), 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL
Authors:Noel, J.P., Ranganathan, R., Hunter, T.
Deposit date:1998-06-21
Release date:1998-10-14
Modification date:2013-04-24
Cite:Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.
Cell(Cambridge,Mass.), 89, 1997
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
Modification date:2009-02-24
Cite:The Structure of the Candida albicans Ess1 Prolyl Isomerase Reveals a Well-Ordered Linker that Restricts Domain Mobility
Biochemistry, 44, 2005
1ZCN
HUMAN PIN1 NG MUTANT
Descriptor:Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8)
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
Modification date:2009-02-24
Cite:Structure-function-folding relationship in a WW domain.
Proc.Natl.Acad.Sci.Usa, 103, 2006
1ZK6
NMR SOLUTION STRUCTURE OF B. SUBTILIS PRSA PPIASE
Descriptor:Foldase protein prsA (E.C.5.2.1.8)
Authors:Tossavainen, H., Permi, P., Purhonen, S.L., Sarvas, M., Kilpelainen, I., Seppala, R.
Deposit date:2005-05-02
Release date:2006-03-28
Modification date:2009-02-24
Cite:NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis
Febs Lett., 580, 2006
2F21
HUMAN PIN1 FIP MUTANT
Descriptor:Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8)
Authors:Jager, M., Zhang, Y., Bowman, M.E., Noel, J.P., Kelly, J.W.
Deposit date:2005-11-15
Release date:2006-06-20
Modification date:2009-02-24
Cite:Structure-function-folding relationship in a WW domain.
Proc.Natl.Acad.Sci.Usa, 103, 2006
2ITK
HUMAN PIN1 BOUND TO D-PEPTIDE
Descriptor:Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8), D-Peptide
Authors:Noel, J.P., Zhang, Y.
Deposit date:2006-10-19
Release date:2007-05-22
Modification date:2011-07-13
Cite:Structural basis for high-affinity peptide inhibition of human Pin1.
Acs Chem.Biol., 2, 2007
2JZV
SOLUTION STRUCTURE OF S. AUREUS PRSA-PPIASE
Descriptor:PrsA-PPIase (E.C.5.2.1.8)
Authors:Seppala, R., Tossavainen, H., Heikkinen, S., Koskela, H., Kontinen, V., Permi, P.
Deposit date:2008-01-21
Release date:2009-01-20
Modification date:2009-03-31
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
2KGJ
SOLUTION STRUCTURE OF PARVULIN DOMAIN OF PPID FROM E.COLI
Descriptor:Peptidyl-prolyl cis-trans isomerase D (E.C.5.2.1.8)
Authors:Weininger, U., Jakob, R.P.
Deposit date:2009-03-12
Release date:2010-01-19
Cite:The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity.
Protein Sci., 19, 2009
2LJ4
SOLUTION STRUCTURE OF THE TBPIN1
Descriptor:Peptidyl-prolyl cis-trans isomerase/rotamase, putative (E.C.5.2.1.8)
Authors:Sun, L., Lin, D., Zhao, Y.
Deposit date:2011-09-06
Release date:2012-08-22
Cite:Solution Structural Analysis of the Single-Domain Parvulin TbPin1
Plos One, 7, 2012
2PV1
CRYSTALLOGRAPHIC STRUCTURE OF SURA FIRST PEPTIDYL-PROLYL ISOMERASE DOMAIN COMPLEXED WITH PEPTIDE WEYIPNV
Descriptor:Chaperone surA (E.C.5.2.1.8), Glycosyl transferase, group 1
Authors:Xu, X., McKay, D.B.
Deposit date:2007-05-09
Release date:2007-10-02
Modification date:2009-02-24
Cite:The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues.
J.Mol.Biol., 373, 2007
2PV2
CRYSTALLOGRAPHIC STRUCTURE OF SURA FIRST PEPTIDYL-PROLYL ISOMERASE DOMAIN COMPLEXED WITH PEPTIDE NFTLKFWDIFRK
Descriptor:Chaperone surA (E.C.5.2.1.8), C-peptide
Authors:Xu, X., McKay, D.B.
Deposit date:2007-05-09
Release date:2007-10-02
Modification date:2009-02-24
Cite:The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues.
J.Mol.Biol., 373, 2007
2PV3
CRYSTALLOGRAPHIC STRUCTURE OF SURA FRAGMENT LACKING THE SECOND PEPTIDYL-PROLYL ISOMERASE DOMAIN COMPLEXED WITH PEPTIDE NFTLKFWDIFRK
Descriptor:Chaperone surA (E.C.5.2.1.8), C-peptide
Authors:Xu, X., McKay, D.B.
Deposit date:2007-05-09
Release date:2007-10-02
Modification date:2011-07-13
Cite:The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues.
J.Mol.Biol., 373, 2007
2Q5A
HUMAN PIN1 BOUND TO L-PEPTIDE
Descriptor:Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8), Five residue peptide
Authors:Noel, J.P., Zhang, Y.
Deposit date:2007-05-31
Release date:2007-06-26
Modification date:2011-07-13
Cite:Structural basis for high-affinity peptide inhibition of human Pin1.
Acs Chem.Biol., 2, 2007
2RQS
3D STRUCTURE OF PIN FROM THE PSYCHROPHILIC ARCHEON CENARCHEAUM SYMBIOSUM (CSPIN)
Descriptor:Parvulin-like peptidyl-prolyl isomerase (E.C.5.2.1.8)
Authors:Zhukov, I., Jaremko, L., Jaremko, M., Mueller, J.W., Bayer, P.
Deposit date:2009-11-17
Release date:2010-11-24
Modification date:2011-03-23
Cite:Structure and Dynamics of the First Archaeal Parvulin Reveal a New Functionally Important Loop in Parvulin-type Prolyl Isomerases
J.Biol.Chem., 286, 2011
2XP3
DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
Descriptor:PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1 (E.C.5.2.1.8)
Authors:Potter, A., Oldfield, V., Nunns, C., Fromont, C., Ray, S., Northfield, C.J., Bryant, C.J., Scrace, S.F., Robinson, D., Matossova, N., Baker, L., Dokurno, P., Surgenor, A.E., Davis, B.E., Richardson, C.M., Murray, J.B., Moore, J.D.
Deposit date:2010-08-25
Release date:2011-01-12
Cite:Discovery of Cell-Active Phenyl-Imidazole Pin1 Inhibitors by Structure-Guided Fragment Evolution.
Bioorg.Med.Chem.Lett., 20, 2010
2XP4
DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
Descriptor:PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1 (E.C.5.2.1.8)
Authors:Potter, A., Oldfield, V., Nunns, C., Fromont, C., Ray, S., Northfield, C.J., Bryant, C.J., Scrace, S.F., Robinson, D., Matossova, N., Baker, L., Dokurno, P., Surgenor, A.E., Davis, B.E., Richardson, C.M., Murray, J.B., Moore, J.D.
Deposit date:2010-08-25
Release date:2011-01-12
Cite:Discovery of Cell-Active Phenyl-Imidazole Pin1 Inhibitors by Structure-Guided Fragment Evolution.
Bioorg.Med.Chem.Lett., 20, 2010
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