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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
|
| pubmed:dateCreated |
1995-3-15
|
| pubmed:abstractText |
Triple-stranded laminin molecules assemble via an alpha-helical coiled-coil structure spanning approximately 600 amino acid residues of each chain. We reported that the C termini of the beta 1 and gamma 1 chains direct the specific dimer and trimer assembly (Utani, A., Nomizu, M., Timpl, R., Roller, P.P., and Yamada, Y. (1994) J. Biol. Chem. 269, 19167-19175). In this study, we focused on the mechanism of trimer formation of the alpha 2 chain utilizing three different approaches. First, competition assays using mutated recombinant alpha 2 chain defined a 25-amino acid sequence at the C terminus of the long arm as an essential site for assembly with beta 1 and gamma 1 chain. Site-specific mutations and synthetic peptides of this site revealed that both positively charged amino acid residues and the alpha-helical structure within this site were critical. Second, overexpression studies of recombinant alpha 2 chain long arm confirmed that the C-terminal end was critical for the trimer assembly within NIH 3T3 cells. Third, circular dichroism spectroscopic examination of the complexes reconstituted in vitro revealed dynamic conformational changes of the alpha 2 and gamma 1 chains in the process of assembly. These studies also revealed that the proper folding of the extreme C terminus of alpha 2 chain was critical for the stability of trimer. From these data, it is concluded that the C terminus of alpha 2 chain long arm is required for the effective initiation of laminin heterotrimer assembly.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
17
|
| pubmed:volume |
270
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
3292-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7852414-3T3 Cells,
pubmed-meshheading:7852414-Amino Acid Sequence,
pubmed-meshheading:7852414-Animals,
pubmed-meshheading:7852414-Animals, Newborn,
pubmed-meshheading:7852414-Chromatography, Affinity,
pubmed-meshheading:7852414-Circular Dichroism,
pubmed-meshheading:7852414-Cloning, Molecular,
pubmed-meshheading:7852414-Laminin,
pubmed-meshheading:7852414-Macromolecular Substances,
pubmed-meshheading:7852414-Mice,
pubmed-meshheading:7852414-Molecular Sequence Data,
pubmed-meshheading:7852414-Mutagenesis, Site-Directed,
pubmed-meshheading:7852414-Myocardium,
pubmed-meshheading:7852414-Peptides,
pubmed-meshheading:7852414-Point Mutation,
pubmed-meshheading:7852414-Protein Conformation,
pubmed-meshheading:7852414-Protein Processing, Post-Translational,
pubmed-meshheading:7852414-Protein Structure, Secondary,
pubmed-meshheading:7852414-Recombinant Fusion Proteins,
pubmed-meshheading:7852414-Recombinant Proteins,
pubmed-meshheading:7852414-Sequence Homology, Amino Acid,
pubmed-meshheading:7852414-Transfection
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
A specific sequence of the laminin alpha 2 chain critical for the initiation of heterotrimer assembly.
|
| pubmed:affiliation |
Laboratory of Developmental Biology, NIDR, National Institutes of Health, Bethesda, Maryland 20892.
|
| pubmed:publicationType |
Journal Article,
Comparative Study
|