000054327 001__ 54327
000054327 005__ 20200402210243.0
000054327 0247_ $$2pmid$$apmid:17045295
000054327 0247_ $$2DOI$$a10.1016/j.jmb.2006.09.052
000054327 0247_ $$2WOS$$aWOS:000242674200019
000054327 037__ $$aPreJuSER-54327
000054327 041__ $$aeng
000054327 082__ $$a570
000054327 084__ $$2WoS$$aBiochemistry & Molecular Biology
000054327 1001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b0$$uFZJ
000054327 245__ $$aCrystal structure of a multi-domain immunophilin from Arabidopsis thaliana: A paradigm for regulation of plan ABC transporters
000054327 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2006
000054327 300__ $$a799 - 809
000054327 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000054327 3367_ $$2DataCite$$aOutput Types/Journal article
000054327 3367_ $$00$$2EndNote$$aJournal Article
000054327 3367_ $$2BibTeX$$aARTICLE
000054327 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000054327 3367_ $$2DRIVER$$aarticle
000054327 440_0 $$03552$$aJournal of Molecular Biology$$v364$$x0022-2836
000054327 500__ $$aRecord converted from VDB: 12.11.2012
000054327 520__ $$aFKBP42 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.
000054327 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000054327 588__ $$aDataset connected to Web of Science, Pubmed
000054327 650_2 $$2MeSH$$aATP-Binding Cassette Transporters: metabolism
000054327 650_2 $$2MeSH$$aArabidopsis Proteins: chemistry
000054327 650_2 $$2MeSH$$aCrystallography, X-Ray
000054327 650_2 $$2MeSH$$aCytoplasm
000054327 650_2 $$2MeSH$$aHSP90 Heat-Shock Proteins: metabolism
000054327 650_2 $$2MeSH$$aImmunophilins: chemistry
000054327 650_2 $$2MeSH$$aMolecular Structure
000054327 650_2 $$2MeSH$$aProtein Binding
000054327 650_2 $$2MeSH$$aProtein Conformation
000054327 650_2 $$2MeSH$$aTacrolimus Binding Proteins: chemistry
000054327 650_7 $$00$$2NLM Chemicals$$aATP-Binding Cassette Transporters
000054327 650_7 $$00$$2NLM Chemicals$$aArabidopsis Proteins
000054327 650_7 $$00$$2NLM Chemicals$$aHSP90 Heat-Shock Proteins
000054327 650_7 $$00$$2NLM Chemicals$$aTWD1 protein, Arabidopsis
000054327 650_7 $$0EC 5.2.1.-$$2NLM Chemicals$$aTacrolimus Binding Proteins
000054327 650_7 $$0EC 5.2.1.8$$2NLM Chemicals$$aImmunophilins
000054327 650_7 $$2WoSType$$aJ
000054327 65320 $$2Author$$aFKBP42
000054327 65320 $$2Author$$aArabidopsis thaliana
000054327 65320 $$2Author$$aX-ray crystallography
000054327 65320 $$2Author$$aHSP90
000054327 65320 $$2Author$$aABC transporter
000054327 7001_ $$0P:(DE-Juel1)VDB10480$$aEckhoff, A.$$b1$$uFZJ
000054327 7001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O. H.$$b2$$uFZJ
000054327 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2006.09.052$$gVol. 364, p. 799 - 809$$p799 - 809$$q364<799 - 809$$tJournal of molecular biology$$v364$$x0022-2836$$y2006
000054327 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2006.09.052
000054327 909CO $$ooai:juser.fz-juelich.de:54327$$pVDB
000054327 9131_ $$0G:(DE-Juel1)FUEK409$$bGesundheit$$kP33$$lFunktion und Dysfunktion des Nervensystems$$vFunktion und Dysfunktion des Nervensystems$$x0
000054327 9141_ $$y2006
000054327 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000054327 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
000054327 970__ $$aVDB:(DE-Juel1)85114
000054327 980__ $$aVDB
000054327 980__ $$aConvertedRecord
000054327 980__ $$ajournal
000054327 980__ $$aI:(DE-Juel1)ISB-2-20090406
000054327 980__ $$aUNRESTRICTED
000054327 980__ $$aI:(DE-Juel1)ICS-6-20110106
000054327 981__ $$aI:(DE-Juel1)IBI-7-20200312
000054327 981__ $$aI:(DE-Juel1)ISB-2-20090406
000054327 981__ $$aI:(DE-Juel1)ICS-6-20110106