Wikipedia

Fibronectin type I domain

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.

Fibronectin, type I
Identifiers
SymbolFibrnctn1
PfamPF00039
InterProIPR000083
SMARTSM00058
PROSITEPDOC00965
CDDcd00061
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDBPDB: 1e88​ PDB: 1e8b​ PDB: 1fbr​ PDB: 1o9a​ PDB: 1qgb​ PDB: 1qo6​ PDB: 1tpg​ PDB: 1tpm​ PDB: 1tpn​ PDB: 2fn2​

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

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F12; FN1; HGFAC; PLAT;

References

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  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 4328182.642-646&rft.date=1990&rft_id=https://api.semanticscholar.org/CorpusID:4328182#id-name=S2CID&rft_id=info:pmid/2112232&rft_id=info:doi/10.1038/345642a0&rft.aulast=Campbell&rft.aufirst=ID&rft.au=Baron, M&rft.au=Norman, D&rft.au=Willis, A&rfr_id=info:sid/en.wikipedia.org:Fibronectin type I domain" class="Z3988">
  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 1602484.821-833&rft.date=1992&rft_id=info:doi/10.1016/0022-2836(92)90403-7&rft_id=info:pmid/1602484&rft.aulast=Driscoll&rft.aufirst=PC&rft.au=Harvey, TS&rft.au=Campbell, ID&rft.au=Baron, M&rft.au=Dudgeon, TJ&rft.au=Downing, AK&rft.au=Smith, BO&rfr_id=info:sid/en.wikipedia.org:Fibronectin type I domain" class="Z3988">
  3. ^ 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 7582899.823-833&rft.date=1995&rft_id=info:doi/10.1016/S0969-2126(01)00217-9&rft_id=info:pmid/7582899&rft.aulast=Driscoll&rft.aufirst=PC&rft.au=Campbell, ID&rft.au=Dudgeon, TJ&rft.au=Downing, AK&rft.au=Smith, BO&rft_id=https://doi.org/10.1016%2FS0969-2126%2801%2900217-9&rfr_id=info:sid/en.wikipedia.org:Fibronectin type I domain" class="Z3988">
  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 1900516.5191-5201&rft.date=1991&rft_id=info:pmid/1900516&rft.aulast=Bennett&rft.aufirst=WF&rft.au=Paoni, NF&rft.au=Keyt, BA&rft.au=Botstein, D&rft.au=Presta, L&rft.au=Wurm, FM&rft.au=Zoller, MJ&rft.au=Jones, AJ&rfr_id=info:sid/en.wikipedia.org:Fibronectin type I domain" class="Z3988">
This article incorporates text from the public domain Pfam and InterPro: IPR000083
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