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The crystal structure of the GroES co-chaperonin at 2.8 angstrom resolution
Author(s): Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J
Source: NATURE    Volume: 379    Issue: 6560    Pages: 37-45    Published: JAN 4 1996  
Times Cited: 308     References: 53     
Abstract: The GroES heptamer forms a dome, approximately 75 Angstrom in diameter and 30 Angstrom high, with an 8 Angstrom orifice in the centre of its roof. The 'mobile loop' segment, previously identified as a GroEL binding determinant, is disordered in the crystal structure in six subunits; the single well-ordered copy extends from the bottom outer rim of the GroES dome, suggesting that the cavity within the dome is continuous with the polypeptide binding chamber of GroEL in the chaperonin complex.
Document Type: Article
Language: English
Reprint Address: Hunt, JF (reprint author), UNIV TEXAS, SW MED CTR, HOWARD HUGHES MED INST, DALLAS, TX 75235 USA
Addresses:
1. UNIV TEXAS, SW MED CTR, DEPT BIOCHEM, DALLAS, TX 75235 USA
2. UNIV TEXAS, SW MED CTR, DEPT PHARMACOL, DALLAS, TX 75235 USA
Publisher: MACMILLAN MAGAZINES LTD, 4 LITTLE ESSEX STREET, LONDON, ENGLAND WC2R 3LF
Subject Category: Multidisciplinary Sciences
IDS Number: TN216
ISSN: 0028-0836
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