Fibronectin type I domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	PDB: 1e88 PDB: 1e8b PDB: 1fbr PDB: 1o9a PDB: 1qgb PDB: 1qo6 PDB: 1tpg PDB: 1tpm PDB: 1tpn PDB: 2fn2

Fibronectin, type I
Fibronectin, type I
Identifiers
Symbol	Fibrnctn1
Pfam	PF00039
InterPro	IPR000083
SMART	SM00058
PROSITE	PDOC00965
CDD	cd00061
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	PDB: 1e88 PDB: 1e8b PDB: 1fbr PDB: 1o9a PDB: 1qgb PDB: 1qo6 PDB: 1tpg PDB: 1tpm PDB: 1tpn PDB: 2fn2

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

F12; FN1; HGFAC; PLAT;

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. S2CID 4328182.
^ 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.
^ ^a ^b 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

[PUB00004065-1] 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. S2CID 4328182.

[PUB00003289-2] 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.

[PUB00005265-3] 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.

[PUB00002685-4] 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.

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