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| 001 | 140876 | ||
| 005 | 20240321220907.0 | ||
| 024 | 7 | _ | |a 10.1002/pro.3678 |2 doi |
| 024 | 7 | _ | |a pmid:31299134 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC6699087 |2 pmc |
| 024 | 7 | _ | |a 0961-8368 |2 ISSN |
| 024 | 7 | _ | |a 1469-896X |2 ISSN |
| 024 | 7 | _ | |a altmetric:64130281 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-07198 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Oroz, Javier |0 P:(DE-2719)2810826 |b 0 |e First author |u dzne |
| 245 | _ | _ | |a Dynamic Aha1 co-chaperone binding to human Hsp90. |
| 260 | _ | _ | |a Bethesda, Md. |c 2019 |b Protein Society |
| 264 | _ | 1 | |3 online |2 Crossref |b Wiley |c 2019-08-06 |
| 264 | _ | 1 | |3 print |2 Crossref |b Wiley |c 2019-09-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1624270571_20183 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Hsp90 is an essential chaperone that requires large allosteric changes to determine its ATPase activity and client binding. The co-chaperone Aha1, which is the major ATPase stimulator in eukaryotes, is important for regulation of Hsp90's allosteric timing. Little is known, however, about the structure of the Hsp90/Aha1 complex. Here, we characterize the solution structure of unmodified human Hsp90/Aha1 complex using NMR spectroscopy. We show that the 214-kDa complex forms by a two-step binding mechanism and adopts multiple conformations in the absence of nucleotide. Aha1 induces structural changes near Hsp90's nucleotide-binding site, providing a basis for its ATPase-enhancing activity. Our data reveal important aspects of this pivotal chaperone/co-chaperone interaction and emphasize the relevance of characterizing dynamic chaperone structures in solution. |
| 536 | _ | _ | |a 342 - Disease Mechanisms and Model Systems (POF3-342) |0 G:(DE-HGF)POF3-342 |c POF3-342 |f POF III |x 0 |
| 542 | _ | _ | |i 2019-08-06 |2 Crossref |u http://creativecommons.org/licenses/by/4.0/ |
| 542 | _ | _ | |i 2019-08-06 |2 Crossref |u http://doi.wiley.com/10.1002/tdm_license_1.1 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 2 | |a Allosteric Regulation |2 MeSH |
| 650 | _ | 2 | |a Binding Sites |2 MeSH |
| 650 | _ | 2 | |a HSP90 Heat-Shock Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a HSP90 Heat-Shock Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Models, Molecular |2 MeSH |
| 650 | _ | 2 | |a Molecular Chaperones: chemistry |2 MeSH |
| 650 | _ | 2 | |a Molecular Chaperones: metabolism |2 MeSH |
| 650 | _ | 2 | |a Molecular Weight |2 MeSH |
| 650 | _ | 2 | |a Nuclear Magnetic Resonance, Biomolecular |2 MeSH |
| 650 | _ | 2 | |a Protein Binding |2 MeSH |
| 650 | _ | 2 | |a Protein Conformation |2 MeSH |
| 700 | 1 | _ | |a Blair, Laura J |b 1 |
| 700 | 1 | _ | |a Zweckstetter, Markus |0 P:(DE-2719)2810591 |b 2 |e Last author |u dzne |
| 773 | 1 | 8 | |a 10.1002/pro.3678 |b : Wiley, 2019-08-06 |n 9 |p 1545-1551 |3 journal-article |2 Crossref |t Protein Science |v 28 |y 2019 |x 0961-8368 |
| 773 | _ | _ | |a 10.1002/pro.3678 |g Vol. 28, no. 9, p. 1545 - 1551 |0 PERI:(DE-600)2000025-X |n 9 |q 28:9<1545 - 1551 |p 1545-1551 |t Protein science |v 28 |y 2019 |x 0961-8368 |
| 856 | 4 | _ | |y OpenAccess |u https://pub.dzne.de/record/140876/files/5361.pdf |
| 856 | 4 | _ | |y OpenAccess |x pdfa |u https://pub.dzne.de/record/140876/files/5361.pdf?subformat=pdfa |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6699087 |
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| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 0 |6 P:(DE-2719)2810826 |
| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 2 |6 P:(DE-2719)2810591 |
| 913 | 1 | _ | |a DE-HGF |b Gesundheit |l Erkrankungen des Nervensystems |1 G:(DE-HGF)POF3-340 |0 G:(DE-HGF)POF3-342 |3 G:(DE-HGF)POF3 |2 G:(DE-HGF)POF3-300 |4 G:(DE-HGF)POF |v Disease Mechanisms and Model Systems |x 0 |
| 913 | 2 | _ | |a DE-HGF |b Programmungebundene Forschung |l ohne Programm |1 G:(DE-HGF)POF4-890 |0 G:(DE-HGF)POF4-899 |3 G:(DE-HGF)POF4 |2 G:(DE-HGF)POF4-800 |4 G:(DE-HGF)POF |v ohne Topic |x 0 |
| 914 | 1 | _ | |y 2019 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |d 2022-11-26 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1050 |2 StatID |b BIOSIS Previews |d 2022-11-26 |
| 915 | _ | _ | |a Creative Commons Attribution CC BY 4.0 |0 LIC:(DE-HGF)CCBY4 |2 HGFVOC |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |b PROTEIN SCI : 2021 |d 2022-11-26 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |d 2022-11-26 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1030 |2 StatID |b Current Contents - Life Sciences |d 2022-11-26 |
| 915 | _ | _ | |a OpenAccess |0 StatID:(DE-HGF)0510 |2 StatID |
| 915 | _ | _ | |a IF >= 5 |0 StatID:(DE-HGF)9905 |2 StatID |b PROTEIN SCI : 2021 |d 2022-11-26 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |d 2022-11-26 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Clarivate Analytics Master Journal List |d 2022-11-26 |
| 920 | 1 | _ | |0 I:(DE-2719)1410001 |k AG Zweckstetter |l Structural Biology in Dementia |x 0 |
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