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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1998-11-17
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pubmed:abstractText |
Application of computer methods allowed us to demonstrate that plant peroxidases and auxin-binding proteins contain structurally similar fragments. The mapping of the fragments was done using a model structure of horseradish peroxidase. Five of six structurally similar fragments belong to the distal domain and form a subdomain in plant peroxidases that includes the distal heme-coordinating sequence, LHFHDC (amino acid residues 39-44 in horseradish peroxidase). The existence of a substrate-binding site for indole-3-acetic acid in the distal subdomain comprising helices A (whole), B (middle), C (beginning), and D (whole) and the loop between helices D and D' is discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2979
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
629-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9668202-Amino Acid Sequence,
pubmed-meshheading:9668202-Indoleacetic Acids,
pubmed-meshheading:9668202-Molecular Sequence Data,
pubmed-meshheading:9668202-Peroxidases,
pubmed-meshheading:9668202-Plant Growth Regulators,
pubmed-meshheading:9668202-Plant Proteins,
pubmed-meshheading:9668202-Plants,
pubmed-meshheading:9668202-Protein Conformation,
pubmed-meshheading:9668202-Receptors, Cell Surface,
pubmed-meshheading:9668202-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Evidence for indole-3-acetic acid binding site in plant peroxidases. Structural similarity between peroxidases and auxin-binding proteins.
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pubmed:affiliation |
Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia.
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pubmed:publicationType |
Journal Article
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