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PREDICTING COILED COILS FROM PROTEIN SEQUENCES
Author(s): LUPAS A, VANDYKE M, STOCK J
Source: SCIENCE    Volume: 252    Issue: 5009    Pages: 1162-1164    Published: MAY 24 1991  
Times Cited: 2,254     References: 31     
Abstract: The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta-subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.
Document Type: Article
Language: English
Addresses:
1. PRINCETON UNIV, DEPT MOLEC BIOL, PRINCETON, NJ 08544 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005
Subject Category: Multidisciplinary Sciences
IDS Number: FN056
ISSN: 0036-8075
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