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CRYSTAL-STRUCTURE OF TFIID TATA-BOX BINDING-PROTEIN
Author(s): NIKOLOV DB, HU SH, LIN J, GASCH A, HOFFMANN A, HORIKOSHI M, CHUA NH, ROEDER RG, BURLEY SK
Source: NATURE    Volume: 360    Issue: 6399    Pages: 40-46    Published: NOV 5 1992  
Times Cited: 305     References: 67     
Abstract: The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDtau) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 angstrom resolution. This highly symmetric alpha/beta structure contains a new DNA-binding fold, resembling a molecular 'saddle' that sits astride the DNA. The DNA-binding surface is a curved, antiparallel beta-sheet. When bound to DNA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.
Document Type: Article
Language: English
Addresses:
1. ROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USA
2. ROCKEFELLER UNIV, PLANT MOLEC BIOL LAB, NEW YORK, NY 10021 USA
3. ROCKEFELLER UNIV, BIOCHEM & MOLEC BIOL LAB, NEW YORK, NY 10021 USA
4. ROCKEFELLER UNIV, HOWARD HUGHES MED INST, NEW YORK, NY 10021 USA
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: JW717
ISSN: 0028-0836
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