دورية أكاديمية
Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.
| العنوان: | Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. |
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| المؤلفون: | Grüne T; European Molecular Biology Laboratory, Grenoble Outstation, B.P. 181, F 38042 Grenoble 9, France., Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Müller CW |
| المصدر: | Molecular cell [Mol Cell] 2003 Aug; Vol. 12 (2), pp. 449-60. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Cell Press Country of Publication: United States NLM ID: 9802571 Publication Model: Print Cited Medium: Print ISSN: 1097-2765 (Print) Linking ISSN: 10972765 NLM ISO Abbreviation: Mol Cell Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Cambridge Ma : Cell Press Original Publication: Cambridge, Mass. : Cell Press, c1997- |
| مواضيع طبية MeSH: | Adenosine Triphosphatases/*metabolism , Nucleosomes/*metabolism , Transcription Factors/*metabolism, Adenosine Triphosphatases/chemistry ; Amino Acid Sequence ; Animals ; Binding Sites ; Chromatin/metabolism ; Crystallography, X-Ray ; Drosophila melanogaster/metabolism ; Gene Deletion ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Proto-Oncogene Proteins c-myb/metabolism ; Sequence Homology, Amino Acid ; Time Factors |
| مستخلص: | Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two alpha-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate. |
| سلسلة جزيئية: | PDB 1OFC |
| المشرفين على المادة: | 0 (Chromatin) 0 (ISWI protein) 0 (Nucleosomes) 0 (Proto-Oncogene Proteins c-myb) 0 (Transcription Factors) EC 3.6.1.- (Adenosine Triphosphatases) |
| تواريخ الأحداث: | Date Created: 20031011 Date Completed: 20031125 Latest Revision: 20190917 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/s1097-2765(03)00273-9 |
| PMID: | 14536084 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1097-2765 |
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| DOI: | 10.1016/s1097-2765(03)00273-9 |