|PROSITE documentation PDOC00965|
Fibronectin is a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. The major part of the sequence of fibronectin consists of the repetition of three types of domains, which are called type I, II, and III . Type I domain (FN1) is approximately 40 residues in length. Four conserved cysteines are involved in disulfide bonds. Fibronectin contains 12 repeats of this domain.
The 3D structure of the FN1 domain has been determined (see <PDB:1FBR>) [2,3,4,5]. It consists of two antiparallel β-sheets, first a double-stranded one, that is linked by a disulfide bond to a triple-stranded β-sheet. The second conserved disulfide bridge links the C-terminal adjacent strands of the domain (see the schematic representation below).
+--------+ +---------------------------|-+ | | | | | xxCxxxxxxxxaxxxxxax+xxxxxxxxxxCxCxxxxxxCxxx ************************************** bbb bbb bbbbb bbbbb bbbbb
'C': conserved cysteine involved in a disulfide bond. 'a': often conserved aromatic amino acid. 'b': position of sheet-forming amino acids. '+': positively charged amino acid. '*': position of the pattern.
In human tissue plasminogen activator chain A, the FN1 domain together with the following epidermal growth factor (EGF)-like domain (see <PDOC00021>) are involved in fibrin-binding . It has been suggested that these two modules form a single structural and functional unit . The two domains keep their specific tertiary structure, but interact intimately to bury a hydrophobic core; the inter-module linker makes up the third strand of the EGF-module's major β-sheet.
The FN1 domain is also found as a single copy in the following mammalian proteins:
We developed a pattern, that spans the domain between the first and the last conserved cysteine. We also developed a profile that covers the whole FN1 domain.Note:
The pattern will, in a few cases, miss one of the FN1 domains in fibronectin due to rare further variation in gap length or lack of one of the conserved aromatic amino acids.Expert(s) to contact by email:
March 2005 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Skorstengaard K. Jensen M.S. Sahl P. Petersen T.E. Magnusson S.|
|Title||Complete primary structure of bovine plasma fibronectin.|
|Source||Eur. J. Biochem. 161:441-453(1986).|
|2||Authors||Baron M. Norman D. Willis A. Campbell I.D.|
|Title||Structure of the fibronectin type 1 module.|
|3||Authors||Downing A.K. Driscoll P.C. Harvey T.S. Dudgeon T.J. Smith B.O. Baron M. Campbell I.D.|
|Title||Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance.|
|Source||J. Mol. Biol. 225:821-833(1992).|
|4||Authors||Smith B.O. Downing A.K. Driscoll P.C. Dudgeon T.J. Campbell I.D.|
|Title||The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator.|
|5||Authors||Potts J.R. Phan I. Williams M.J. Campbell I.D.|
|Source||Nat. Genet. 2:946-950(1995).|
|6||Authors||Bennett W.F. Paoni N.F. Keyt B.A. Botstein D. Jones A.J.S. Presta L. Wurm F.M. Zoller M.J.|
|Title||High resolution analysis of functional determinants on human tissue-type plasminogen activator.|
|Source||J. Biol. Chem. 266:5191-5201(1991).|