Peptidyl-prolyl Cis/Trans isomerases:
Gespeichert in:
| Hauptverfasser: | , |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Oxford [u.a.]
Oxford University Press
1998
|
| Schriftenreihe: | Protein profile
|
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | 117 S. graph. Darst. |
| ISBN: | 0198502885 |
Internformat
MARC
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| 100 | 1 | |a Galat, Andrezj |e Verfasser |4 aut | |
| 245 | 1 | 0 | |a Peptidyl-prolyl Cis/Trans isomerases |c Andrzej Galat ; Sylvie Rivière |
| 264 | 1 | |a Oxford [u.a.] |b Oxford University Press |c 1998 | |
| 300 | |a 117 S. |b graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 490 | 0 | |a Protein profile | |
| 650 | 7 | |a Isomérase |2 ram | |
| 650 | 4 | |a Peptidylprolyl Isomerase |x chemistry | |
| 650 | 4 | |a Peptidylprolyl Isomerase |x genetics | |
| 650 | 4 | |a Peptidylprolyl isomerase | |
| 650 | 0 | 7 | |a cis-trans-Isomerie |0 (DE-588)4148046-6 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Peptidylprolylisomerasen |g Peptidylprolyl-cis-trans-Isomerasen |0 (DE-588)4541544-4 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Cyclophilin |0 (DE-588)4332417-4 |2 gnd |9 rswk-swf |
| 689 | 0 | 0 | |a Cyclophilin |0 (DE-588)4332417-4 |D s |
| 689 | 0 | 1 | |a cis-trans-Isomerie |0 (DE-588)4148046-6 |D s |
| 689 | 0 | |5 DE-604 | |
| 689 | 1 | 0 | |a Peptidylprolylisomerasen |g Peptidylprolyl-cis-trans-Isomerasen |0 (DE-588)4541544-4 |D s |
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| 700 | 1 | |a Rivière, Sylvie |e Verfasser |4 aut | |
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Datensatz im Suchindex
| _version_ | 1804126616830345216 |
|---|---|
| adam_text | Contents
List of abbreviations xi
Introduction 1
Discovery of PPIases 2
What roles may PPIases play in nature? 3
Do proline residues in proteins have special roles? 4
Sequence analysis of PPIases 7
Cyclophilins 7
Mammalian cyclophilins; Plant cyclophilins; Cyclophilins from
invertebrates and parasites; Cyclophilins from fungi and slime moulds;
Cyclophilins from prokaryotes
FK506 binding proteins 20
Mammalian FKBPs; FKBPs from fungi and plants; FKBPs from
invertebrates and parasites; FKBPs from prokaryotes
Trigger factor has PPIase activity 29
Parvulins 29
Correlations between the functions and sequences of four
families of PPIases 30
Genes and the cellular localization of PPIases 32
Genomic organization of mammalian PPIases and associated
proteins 32
Localization of major PPIases in eukaryotic cells 32
Secreted forms of PPIases 33
Genes of prokaryotic PPIases 34
Proteins interacting with PPIases 36
Cyclophilins and the HIV Gag polyprotein 36
Molecular channels 37
Transcription of genes 38
Steroid hormone receptors 38
In vivo folding and assembly of proteins 39
Intracellularsignallingpathwaysand PPIases 41
Immunophilins and suppression of T cells 41
The cell cycle and immunophilins 46
Ligand binding to PPIases 49
The cyclic peptides—cyclosporins 49
The macrolides—FK506, rapamycin and their homologues 50
The mechanism of ligand binding to PPIases 51
I
Structural analysis of PPlases 53
Cyclophilins and their ligands 53
FKBPs and their complexes with macrolides 55
Complexes of PPIases and their protein ligands 57
Biology of PPIases 58
Methods 62
Bibliography 65
Reviews (references 1 56); Introduction (references 57 77); Sequences of PPIs
(references 78 291); Genes and cellular localization of PPIs (references 292 355);
Other interacting proteins (references 356—458); Intracellular signalling pathway
and PPIases (references 459 630); Inhibitors of PPIs (references 631 716);
3D structure of PPIases (references 717 797); Biology of PPIases
(references 798 911); Methods (references 912 926)
Appendix 1: Protein databases and their structure 102
Appendix 2: Hydrophobicity plots 104
Appendix 3: Analysis of kinetic data files 108
Appendix4: Distribution of X Pro Ytriplets in proteins 109
Appendix 5: Protein sequence alignments 111
List of Figures
Figure 1 Schematic representation of cisjtrans isomerization
about a peptidyl prolyl bond catalysed by an
isomerase 2
Figure 2 Convention for the torsion angle u) of trans and
cis peptide bonds 5
Figure 3 Global alignment of the CLDs from nine
mammalian proteins 8
Figure 4 Sequence alignment of human cyclophilin A
with the CLDs from nine unique mammalian
proteins 8
Figure 5 Two dimensional gel of proteins from bovine kidney 11
Figure 6 Schematic representation of the nuclear cyclophilin
hCyP 33 12
Figure 7 Schematic representation of the nuclear cyclophilin
hCyP 58 12
Figure 8 Schematic representation of the nuclear cyclophilin
hCyP 88andhCyP 158 13
Figure 9 Sequence alignment of human cyclophilin A
(hCyP 18) with 11 cyclophilins from ( .. elegant 14
Figure 10 Alignment of the CLD from the 97 kDa
ftrupia malayi protein with those from three other
proteins 17
Figure 11 FKBPs entrapped on FK5O6 or rapamycin affinity
gels 20
Figure 12 Global alignment of six sequences of the FKBP
family of proteins 22
Figure 13 Alignment of the PPlases domains of several
human FKBPs 24
Figure 14 Diagram of FKBP likc domains from
TaFKBP 70r hFKBP 54 and hFKBP 12a 25
Figure 15 Similarities between the FK506 binding
domain of SfFKBP 46 and hFKBP 12ot 26
Figure 16 Sequence alignment of mammalian and
prokaryotic members of the FKBP 25 family 27
Figure 17 Sequence alignment of human FKBP 12 with
fragments of li. coli trigger factor 28
Figure 18 Sequence alignment of human Pinl protein with
several parvulins 28
Figure 19 Global sequence alignment of four members of
the cyclophilin and FKBP families of proteins 30
Figure 20 Diagram of the TPR domains in hFKBP 52 and
bCyP 40 aligned with several other TPR domains 31
Figure 21 Cyclophilin A (hCyP 18) binding domain within
various Gag polyproteins 37
Figure 22 Hypothetical pathway for assembly of active
glucocorticoid receptor 39
Figure 23 Hypothetical representation of signal transduction
cascades induced by antigen presenting cell
interaction with the TCR CD3 and CD28 receptors
in a T cell 42
Figure 24 Interleukin 2 promoter and its binding elements 43
Figure 25 Diagram of the Rel domains in several transcription
factors 45
Figure 26 Calcineurin A and its associated proteins
specifically retained on FKBP 12/FK506 affinity gel 45
Figure 27 Calcineurin A and its domains, and a schematic
representation of putative calcineurin A binding
domain in AKAP 46
Figure 28 FKBP 12/rapamycin associated protein (FRAP) 47 ¦
Figure 29 Ribosomal S6 p70 protein kinase 47
Figure 30 Chemical structure of cyclosporin A 50
Figure 31 Chemical structures of FK506 and rapamycin 51
Figure 32 Ribbon structures of hCyP 18 and FKBP 12 53
Figure A2.1 Hydrophobicity profile of DmCyP 26 105
Figure A2.2 Hydrophobicity profile of hFKBP 12a 105
List of Tables
Table 1 Tentative biological functions of PPIases 3
Table 2 Percentage of proline residues in proteins 4
Table 3 The fraction of X—Pro peptide bonds in proteins 6
Table 4 Cyclophilins from vertebrates 10
Table 5 Cyclophilins from plants 14
Table 6 Cyclophilins from invertebrates and parasites 16
Table 7 Cyclophilins from fungi and slime moulds 18
Table 8 Cyclophilins from prokaryotes 19
Table 9 FKBPs from vertebrates 21
Table 10 FKBPs from plants and fungi 23
Table 11 FKBPs from invertebrates and parasites 25
Table 12 FKBPs from prokaryotes 26
Table 13 The interleukin 2 promoter and its binding proteins 42
Table 14 Data on calcineurin A, B and calmodulin 46
Table 15 Structures of cyclophilins 56
Table 16 Structures of FKBPs 56
Table 17 Some of the biological effects of Cs A 59
Table 18 Some of the biological effects of FK506 60
Table 19 Some of the biological effects of rapamycin 61
Table 20 Methods for immunophilins 62
Table A4.1 Frequency of X Pro Y bonds in proteins 111
|
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| author | Galat, Andrezj Rivière, Sylvie |
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| id | DE-604.BV012018839 |
| illustrated | Illustrated |
| indexdate | 2024-07-09T18:20:17Z |
| institution | BVB |
| isbn | 0198502885 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-008134719 |
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| owner_facet | DE-355 DE-BY-UBR DE-91G DE-BY-TUM DE-11 |
| physical | 117 S. graph. Darst. |
| publishDate | 1998 |
| publishDateSearch | 1998 |
| publishDateSort | 1998 |
| publisher | Oxford University Press |
| record_format | marc |
| series2 | Protein profile |
| spelling | Galat, Andrezj Verfasser aut Peptidyl-prolyl Cis/Trans isomerases Andrzej Galat ; Sylvie Rivière Oxford [u.a.] Oxford University Press 1998 117 S. graph. Darst. txt rdacontent n rdamedia nc rdacarrier Protein profile Isomérase ram Peptidylprolyl Isomerase chemistry Peptidylprolyl Isomerase genetics Peptidylprolyl isomerase cis-trans-Isomerie (DE-588)4148046-6 gnd rswk-swf Peptidylprolylisomerasen Peptidylprolyl-cis-trans-Isomerasen (DE-588)4541544-4 gnd rswk-swf Cyclophilin (DE-588)4332417-4 gnd rswk-swf Cyclophilin (DE-588)4332417-4 s cis-trans-Isomerie (DE-588)4148046-6 s DE-604 Peptidylprolylisomerasen Peptidylprolyl-cis-trans-Isomerasen (DE-588)4541544-4 s Rivière, Sylvie Verfasser aut HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008134719&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Galat, Andrezj Rivière, Sylvie Peptidyl-prolyl Cis/Trans isomerases Isomérase ram Peptidylprolyl Isomerase chemistry Peptidylprolyl Isomerase genetics Peptidylprolyl isomerase cis-trans-Isomerie (DE-588)4148046-6 gnd Peptidylprolylisomerasen Peptidylprolyl-cis-trans-Isomerasen (DE-588)4541544-4 gnd Cyclophilin (DE-588)4332417-4 gnd |
| subject_GND | (DE-588)4148046-6 (DE-588)4541544-4 (DE-588)4332417-4 |
| title | Peptidyl-prolyl Cis/Trans isomerases |
| title_auth | Peptidyl-prolyl Cis/Trans isomerases |
| title_exact_search | Peptidyl-prolyl Cis/Trans isomerases |
| title_full | Peptidyl-prolyl Cis/Trans isomerases Andrzej Galat ; Sylvie Rivière |
| title_fullStr | Peptidyl-prolyl Cis/Trans isomerases Andrzej Galat ; Sylvie Rivière |
| title_full_unstemmed | Peptidyl-prolyl Cis/Trans isomerases Andrzej Galat ; Sylvie Rivière |
| title_short | Peptidyl-prolyl Cis/Trans isomerases |
| title_sort | peptidyl prolyl cis trans isomerases |
| topic | Isomérase ram Peptidylprolyl Isomerase chemistry Peptidylprolyl Isomerase genetics Peptidylprolyl isomerase cis-trans-Isomerie (DE-588)4148046-6 gnd Peptidylprolylisomerasen Peptidylprolyl-cis-trans-Isomerasen (DE-588)4541544-4 gnd Cyclophilin (DE-588)4332417-4 gnd |
| topic_facet | Isomérase Peptidylprolyl Isomerase chemistry Peptidylprolyl Isomerase genetics Peptidylprolyl isomerase cis-trans-Isomerie Peptidylprolylisomerasen Peptidylprolyl-cis-trans-Isomerasen Cyclophilin |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008134719&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT galatandrezj peptidylprolylcistransisomerases AT rivieresylvie peptidylprolylcistransisomerases |