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rdf:type |
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|
lifeskim:mentions |
|
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pubmed:issue |
5
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pubmed:dateCreated |
1994-4-8
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|
pubmed:abstractText |
A systematic screening of sequence databases with a motif hitherto found only in animal and poxvirus proteins has revealed a trail leading back to prokaryotes. Fortuitously, an X-ray structure is available for one of the identified sequences and shows the fundamental fold to be a set of circularly arranged beta sheets. This structure may be very widely distributed throughout the biological world in sialidases and some other enzymes. In bacteria, a mobile noncatalytic domain is often associated with these same enzymes.
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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 |
Mar
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pubmed:issn |
0022-2836
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
236
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1277-82
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8126718-Alcohol Oxidoreductases,
pubmed-meshheading:8126718-Amino Acid Sequence,
pubmed-meshheading:8126718-Animals,
pubmed-meshheading:8126718-Bacteria,
pubmed-meshheading:8126718-Biological Evolution,
pubmed-meshheading:8126718-Drosophila,
pubmed-meshheading:8126718-Fungi,
pubmed-meshheading:8126718-Galactose Oxidase,
pubmed-meshheading:8126718-Molecular Sequence Data,
pubmed-meshheading:8126718-Neuraminidase,
pubmed-meshheading:8126718-Protein Structure, Secondary,
pubmed-meshheading:8126718-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8126718-Sequence Alignment,
pubmed-meshheading:8126718-Sequence Homology, Amino Acid,
pubmed-meshheading:8126718-Viruses
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pubmed:year |
1994
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pubmed:articleTitle |
Drosophila kelch motif is derived from a common enzyme fold.
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pubmed:affiliation |
European Molecular Biological Laboratory, Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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