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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1995-12-12
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pubmed:abstractText |
Leucine-rich repeats are short sequence motifs present in over sixty proteins, all of which appear to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor demonstrated that the repeats correspond to beta-alpha structural units. The recently determined crystal structure of the ribonuclease A-ribonuclease inhibitor complex suggests the basis for the protein-binding function of leucine-rich repeats.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0959-440X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
409-16
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7583641-Animals,
pubmed-meshheading:7583641-Biological Evolution,
pubmed-meshheading:7583641-Humans,
pubmed-meshheading:7583641-Leucine,
pubmed-meshheading:7583641-Protein Binding,
pubmed-meshheading:7583641-Protein Conformation,
pubmed-meshheading:7583641-Proteins,
pubmed-meshheading:7583641-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:7583641-Sequence Analysis
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pubmed:year |
1995
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pubmed:articleTitle |
Proteins with leucine-rich repeats.
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pubmed:affiliation |
St Vincent's Institute of Medical Research, Fitzroy, Australia.
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pubmed:publicationType |
Journal Article,
Review
|