Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1997-6-11
|
| pubmed:databankReference | |
| pubmed:abstractText |
Fibronectin is an extracellular matrix glycoprotein involved in cell adhesion and migration events in a range of important physiological processes. Aberrant adhesion of cells to the matrix may contribute to the breakdown of normal tissue function associated with various diseases. The adhesive properties of fibronectin may be mediated by its interaction with collagen, the most abundant extracellular matrix protein. The collagen-binding activity of fibronectin has been localized to a 42 kDa proteolytic fragment on the basis of this fragment's affinity for denatured collagen (gelatin). This gelatin-binding domain contains the only type 2 (F2) modules found in the protein. The F2 modules of the matrix metalloproteinases MMP2 and MMP9 are responsible for the affinity of these proteins for gelatin. Knowledge of the structure of fibronectin will provide insights into its interactions with other proteins, and will contribute to our understanding of the structure and function of the extracellular matrix, in both normal and disease-altered tissues.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0969-2126
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
359-70
|
| pubmed:dateRevised |
2009-9-29
|
| pubmed:meshHeading |
pubmed-meshheading:9083105-Amino Acid Sequence,
pubmed-meshheading:9083105-Animals,
pubmed-meshheading:9083105-Binding Sites,
pubmed-meshheading:9083105-Cattle,
pubmed-meshheading:9083105-Cell Adhesion,
pubmed-meshheading:9083105-Collagen,
pubmed-meshheading:9083105-Extracellular Matrix,
pubmed-meshheading:9083105-Fibronectins,
pubmed-meshheading:9083105-Gelatin,
pubmed-meshheading:9083105-Humans,
pubmed-meshheading:9083105-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9083105-Models, Molecular,
pubmed-meshheading:9083105-Molecular Sequence Data,
pubmed-meshheading:9083105-Mutagenesis, Site-Directed,
pubmed-meshheading:9083105-Protein Binding,
pubmed-meshheading:9083105-Protein Conformation,
pubmed-meshheading:9083105-Protein Structure, Secondary,
pubmed-meshheading:9083105-Protein Structure, Tertiary,
pubmed-meshheading:9083105-Recombinant Fusion Proteins,
pubmed-meshheading:9083105-Sequence Alignment,
pubmed-meshheading:9083105-Sequence Homology, Amino Acid
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Solution structure of a type 2 module from fibronectin: implications for the structure and function of the gelatin-binding domain.
|
| pubmed:affiliation |
Oxford Centre for Molecular Sciences Department of Biochemistry South Parks Road, Oxford, OX1 3QU, UK.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|