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Structural basis of a phototropin light switch
Author(s): Harper SM, Neil LC, Gardner KH
Source: SCIENCE    Volume: 301    Issue: 5639    Pages: 1541-1544    Published: SEP 12 2003  
Times Cited: 184     References: 29     
Abstract: Phototropins are light-activated kinases important for plant responses to blue light. Light initiates signaling in these proteins by generating a covalent protein . flavin mononucleotide (FMN) adduct within sensory Per-ARNT-Sim ( PAS) domains. We characterized the light-dependent changes of a phototropin PAS domain by solution nuclear magnetic resonance spectroscopy and found that an alpha helix located outside the canonical domain plays a key role in this activation process. Although this helix associates with the PAS core in the dark, photoinduced changes in the domain structure disrupt this interaction. We propose that this mechanism couples light-dependent bond formation to kinase activation and identifies a signaling pathway conserved among PAS domains.
Document Type: Article
Language: English
Reprint Address: Gardner, KH (reprint author), Univ Texas, SW Med Ctr, Dept Biochem, 5323 Harry Hines Blvd, Dallas, TX 75390 USA
Addresses:
1. Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA
2. Univ Texas, SW Med Ctr, Dept Pharmacol, Dallas, TX 75390 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: 720HL
ISSN: 0036-8075
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