Switch to
Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1994-10-28
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pubmed:abstractText |
The secondary structure of a conserved non-collagenous module in alpha 1(V), alpha 1(XI), alpha 1(IX), alpha 1(XII), alpha 1(XIV) and alpha 1(XVI) collagen chains and in proline- and arginine-rich protein was analyzed using different algorithms. The results predict that a common anti-parallel beta-sheet structure composed of nine consensus beta-strands is present in these non-collagenous modules. A model for the packing of these beta-sheets is proposed which suggests that the predicted beta-sheet structure may be involved in molecular recognition functions.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0945-053X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
14
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
233-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7921540-Algorithms,
pubmed-meshheading:7921540-Amino Acid Sequence,
pubmed-meshheading:7921540-Animals,
pubmed-meshheading:7921540-Collagen,
pubmed-meshheading:7921540-Consensus Sequence,
pubmed-meshheading:7921540-Crystallography, X-Ray,
pubmed-meshheading:7921540-Humans,
pubmed-meshheading:7921540-Models, Molecular,
pubmed-meshheading:7921540-Molecular Sequence Data,
pubmed-meshheading:7921540-Molecular Structure,
pubmed-meshheading:7921540-Protein Folding,
pubmed-meshheading:7921540-Protein Structure, Secondary,
pubmed-meshheading:7921540-Sequence Homology, Amino Acid
|
pubmed:year |
1994
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pubmed:articleTitle |
Common topology within a non-collagenous domain of several different collagen types.
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pubmed:affiliation |
Institut de Biologie et de Chimie des Protéines, UPR412-CNRS, Lyon, France.
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pubmed:publicationType |
Journal Article,
Comparative Study
|