Hauptseite > Publikationsdatenbank > Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: A paradigm for regulation of plan ABC transporters > print

001     54327
005     20200402210243.0
024 7 _ |2 pmid
|a pmid:17045295
024 7 _ |2 DOI
|a 10.1016/j.jmb.2006.09.052
024 7 _ |2 WOS
|a WOS:000242674200019
037 _ _ |a PreJuSER-54327
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Granzin, J.
|b 0
|u FZJ
|0 P:(DE-Juel1)131965
245 _ _ |a Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: A paradigm for regulation of plan ABC transporters
260 _ _ |a Amsterdam [u.a.]
|b Elsevier
|c 2006
300 _ _ |a 799 - 809
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Journal of Molecular Biology
|x 0022-2836
|0 3552
|v 364
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a FKBP42 is a membrane-anchored immunophilin playing a critical role in morphogenesis and development of higher plants. We present the X-ray structure of the cytoplasmic portion of FKBP42 comprising both the FKBP-like domain and the TPR domain at 2.85 A resolution. The data shed light on the probable binding modes of key interaction partners, including HSP90 and two classes of ABC transporters. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a ATP-Binding Cassette Transporters: metabolism
650 _ 2 |2 MeSH
|a Arabidopsis Proteins: chemistry
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Cytoplasm
650 _ 2 |2 MeSH
|a HSP90 Heat-Shock Proteins: metabolism
650 _ 2 |2 MeSH
|a Immunophilins: chemistry
650 _ 2 |2 MeSH
|a Molecular Structure
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Tacrolimus Binding Proteins: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a ATP-Binding Cassette Transporters
650 _ 7 |0 0
|2 NLM Chemicals
|a Arabidopsis Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a HSP90 Heat-Shock Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a TWD1 protein, Arabidopsis
650 _ 7 |0 EC 5.2.1.-
|2 NLM Chemicals
|a Tacrolimus Binding Proteins
650 _ 7 |0 EC 5.2.1.8
|2 NLM Chemicals
|a Immunophilins
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a FKBP42
653 2 0 |2 Author
|a Arabidopsis thaliana
653 2 0 |2 Author
|a X-ray crystallography
653 2 0 |2 Author
|a HSP90
653 2 0 |2 Author
|a ABC transporter
700 1 _ |a Eckhoff, A.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB10480
700 1 _ |a Weiergräber, O. H.
|b 2
|u FZJ
|0 P:(DE-Juel1)131988
773 _ _ |a 10.1016/j.jmb.2006.09.052
|g Vol. 364, p. 799 - 809
|p 799 - 809
|q 364<799 - 809
|0 PERI:(DE-600)1355192-9
|t Journal of molecular biology
|v 364
|y 2006
|x 0022-2836
856 7 _ |u http://dx.doi.org/10.1016/j.jmb.2006.09.052
909 C O |o oai:juser.fz-juelich.de:54327
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913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
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914 1 _ |y 2006
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
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981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

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