Co-operative domains in fibronectin.


The melting of human plasma fibronectin and its proteolytic fragments has been studied by scanning microcalorimetry to reveal co-operative structural domains in the molecule. It has been established that each of the two similar polypeptide chains of fibronectin has at least 12 structural domains, which differ in stability, size and function. Many of the domains in the N-terminal half of the polypeptide chains appear to be composed of two homologous repeat modules that co-operate to form a single co-operative unit. In the intact fibronectin molecule, the C-terminal regions of both chains seem to interact forming a stable co-operative block. Study holds ProTherm entries: 7447, 7448, 7449, 7450, 7451, 7452, 7453, 7454, 7455, 7456, 7457, 7458 Extra Details:

Submission Details


Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Tatunashvili LV;Filimonov VV;Privalov PL;Metsis ML;Koteliansky VE;Ingham KC;Medved LV,J. Mol. Biol. (1990) Co-operative domains in fibronectin. PMID:2299666
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Fibronectin P02751 FINC_HUMAN
96.8 Fibronectin P07589 FINC_BOVIN
94.0 Fibronectin Q28275 FINC_CANLF
92.1 Fibronectin Q28377 FINC_HORSE
90.9 Fibronectin Q91400 FINC_NOTVI