Fibronectin type I domain
| Fibronectin, type I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Fibrnctn1 | ||||||||
| Pfam | PF00039 | ||||||||
| InterPro | IPR000083 | ||||||||
| SMART | SM00058 | ||||||||
| PROSITE | PDOC00965 | ||||||||
| CDD | cd00061 | ||||||||
| |||||||||
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 disulfide bonds. The 3D structure of the FN1 domain has been determined.[1][2][3] It consists of two antiparallel beta-sheets, first a double-stranded one, that is linked by a disulfide bond to a triple-stranded beta-sheet. The second conserved disulfide 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.[4] It has been suggested that these two modules form a single structural and functional unit.[3] 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 beta-sheet.
Human proteins containing this domain
References
- ↑ Campbell ID, Baron M, Norman D, Willis A (1990). "Structure of the fibronectin type 1 module". Nature 345 (6276): 642–646. doi:10.1038/345642a0. PMID 2112232.
- ↑ Driscoll PC, Harvey TS, Campbell ID, Baron M, Dudgeon TJ, Downing AK, Smith BO (1992). "Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance". J. Mol. Biol. 225 (3): 821–833. doi:10.1016/0022-2836(92)90403-7. PMID 1602484.
- 1 2 Driscoll PC, Campbell ID, Dudgeon TJ, Downing AK, Smith BO (1995). "The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator". Structure 3 (8): 823–833. doi:10.1016/S0969-2126(01)00217-9. PMID 7582899.
- ↑ Bennett WF, Paoni NF, Keyt BA, Botstein D, Presta L, Wurm FM, Zoller MJ, Jones AJ (1991). "High resolution analysis of functional determinants on human tissue-type plasminogen activator". J. Biol. Chem. 266 (8): 5191–5201. PMID 1900516.
This article incorporates text from the public domain Pfam and InterPro IPR000083