FN1 dimerizes

Stable Identifier
R-HSA-2545196
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Synonyms
Fibronectin dimerizes
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Prior to matrix formation, fibronectin (FN1) exists as a protein dimer. Often the two peptide chains are differentially-spliced variants. The chains are linked by a pair of C-terminal disulfide bonds which are essential for subsequent multimerization (Schwarzbaur 1991). FN1 monomers have a molecular weight of 230-270 kDa depending on the alternative splicing and contain three types of repeating domains, type I, II, and III. Type I and II domains are stabilized by intra-chain disulfide bonds. FN1 dimer binding to alpha5beta1 integrin stimulates self-association.

Literature References
PubMed ID Title Journal Year
2045422 Identification of the fibronectin sequences required for assembly of a fibrillar matrix

Schwarzbauer, JE

J. Cell Biol. 1991
Participants
Participant Of
Orthologous Events
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Created