Source:http://linkedlifedata.com/resource/pubmed/id/10581249
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
23
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| pubmed:dateCreated |
2000-1-31
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| pubmed:abstractText |
Coiled-coil domains are found in a wide variety of proteins, where they typically specify subunit oligomerization. Recently, we have demonstrated that agrin, a multidomain heparan sulfate proteoglycan with a crucial role in the development of the nerve-muscle synapse, binds to the three-stranded coiled-coil domain of laminin-1. The interaction with laminin mediates the integration of agrin into basement membranes. Here we characterize the binding site within the laminin-1 coiled coil in detail. Binding assays with individual laminin-1 full-length chains and fragments revealed that agrin specifically interacts with the gamma1 subunit of laminin-1, whereas no binding to alpha1 and beta1 chains was detected. By using recombinant gamma1 chain fragments, we mapped the binding site to a sequence of 20 residues. Furthermore, we demonstrate that a coiled-coil conformation of this binding site is required for its interaction with agrin. The finding that recombinant gamma1 fragments bound at least 10-fold less than native laminin-1 indicates that the structure of the three-stranded coiled-coil domain of laminin is required for high-affinity agrin binding. Interestingly, no binding to a chimeric gamma2 fragment was observed, indicating that the interaction of agrin with laminin is isoform specific.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Agrin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/laminin 1
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
|
| pubmed:issn |
0261-4189
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
18
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6762-70
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| pubmed:dateRevised |
2008-11-20
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| pubmed:meshHeading |
pubmed-meshheading:10581249-Agrin,
pubmed-meshheading:10581249-Amino Acid Sequence,
pubmed-meshheading:10581249-Animals,
pubmed-meshheading:10581249-Binding Sites,
pubmed-meshheading:10581249-COS Cells,
pubmed-meshheading:10581249-Circular Dichroism,
pubmed-meshheading:10581249-DNA, Complementary,
pubmed-meshheading:10581249-Escherichia coli,
pubmed-meshheading:10581249-Gene Deletion,
pubmed-meshheading:10581249-Laminin,
pubmed-meshheading:10581249-Molecular Sequence Data,
pubmed-meshheading:10581249-Protein Binding,
pubmed-meshheading:10581249-Protein Conformation,
pubmed-meshheading:10581249-Protein Structure, Tertiary,
pubmed-meshheading:10581249-Recombinant Proteins,
pubmed-meshheading:10581249-Sequence Homology, Amino Acid,
pubmed-meshheading:10581249-Temperature,
pubmed-meshheading:10581249-Transfection,
pubmed-meshheading:10581249-Ultracentrifugation
|
| pubmed:year |
1999
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| pubmed:articleTitle |
Interaction of agrin with laminin requires a coiled-coil conformation of the agrin-binding site within the laminin gamma1 chain.
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| pubmed:affiliation |
Departments of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|