Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding,期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding,

Institution:	3. Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty kopec 7, 656 53 Brno, Czech Republic;;4. BioCeV - Institute of Microbiology of the Czech Academy of Sciences, v.v.i., Prumyslova 595, 252 50 Vestec, Czech Republic;;5. Department of Biochemistry, Faculty of Science, Charles University in Prague, Hlavova 8, 128 43 Prague, Czech Republic;;6. Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France;

Abstract:	Download : Download high-res image (115KB) Download : Download full-size image Highlights ?Hsp70 homologs differ in their oligomeric properties in the presence of ATP. ?Human inducible Hsp70 forms ATP-dependent anti-parallel dimers with high propensity. ?Dimerization of ATP-bound Hsp70 is required for effective Hsp70-Hsp40 interaction. ?ATP-dependent interaction with Tomm34 TPR cochaperone disrupts Hsp70 dimer.

Keywords:	Chaperone Structural Biology Mass Spectrometry Protein Conformation Protein Structure Protein-Protein Interactions Allostery Cochaperone
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