| Description | Fibronectin type I repeats are one of the three repeats found in the fibronectin protein. Fibronectin is a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Type I domain (FN1) is approximately 40 residues in length. Four conserved cysteines are involved in disulphide bonds. The 3D structure of the FN1 domain has been determined [ , , ]. It consists of two antiparallel β-sheets, first a double-stranded one, that is linked by a disulphide bond to a triple-stranded β-sheet. The second conserved disulphide bridge links the C-terminal adjacent strands of the domain.In human tissue plasminogen activator chain A the FN1 domain together with the following epidermal growth factor (EGF)-like domain 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. | Name | Fibronectin, type I |
| Short Name | Fibronectin_type1 | Type | Domain |
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