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Fibronectin type III domain

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This is an old revision of this page, as edited by 216.165.126.18 (talk) at 21:23, 29 August 2019 (Edit corrects the language used in the Monobody description, and adds further detail as to the purpose of these molecules in relation to the fibronection type III domain.). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Fibronectin type III domain
The tenth type III domain of fibronectin
Identifiers
Symbolfn3
PfamPF00041
Pfam clanCL0159
InterProIPR003961
SMARTFN3
PROSITEPDOC00214
SCOP21ttf / SCOPe / SUPFAM
CDDcd00063
Membranome66
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The Fibronectin type III domain is an evolutionary conserved protein domain that is widely found in animal proteins. The fibronectin protein in which this domain was first identified contains 16 copies of this domain. The domain is about 100 amino acids long and possesses a beta sandwich structure. Of the three fibronectin-type domains, type III is the only one without disulfide bonding present. Fibronectin domains are found in a wide variety of extracellular proteins. They are widely distributed in animal species, but also found sporadically in yeast, plant and bacterial proteins.

Human proteins containing this domain

ABI3BP; ANKFN1; ASTN2; AXL; BOC; BZRAP1; C20orf75; CDON; CHL1; CMYA5; CNTFR; CNTN1; CNTN2; CNTN3; CNTN4; CNTN5; CNTN6; COL12A1; COL14A1; COL20A1; COL7A1; CRLF1; CRLF3; CSF2RB; CSF3R; DCC; DSCAM; DSCAML1; EBI3; EGFLAM; EPHA1; EPHA10; EPHA2; EPHA3; EPHA4; EPHA5; EPHA6; EPHA7; EPHA8; EPHB1; EPHB2; EPHB3; EPHB4; EPHB6; EPOR; FANK1; FLRT1; FLRT2; FLRT3; FN1; FNDC1; FNDC3A; FNDC3B; FNDC4; FNDC5; FNDC7; FNDC8; FSD1; FSD1L; FSD2; GHR; HCFC1; HCFC2; HUGO; IFNGR2; IGF1R; IGSF22; IGSF9; IGSF9B; IL4R; IL11RA; IL12B; IL12RB1; IL12RB2; IL20RB; IL23R; IL27RA; IL31RA; IL6R; IL6ST; IL7R; INSR; INSRR; ITGB4; Il6ST; KAL1; KALRN; L1CAM; LEPR; LIFR; LRFN2; LRFN3; LRFN4; LRFN5; LRIT1; LRRN1; LRRN3; MERTK; MID1; MID2; MPL; MYBPC1; MYBPC2; MYBPC3; MYBPH; MYBPHL; MYLK; MYOM1; MYOM2; MYOM3; NCAM1; NCAM2; NEO1; NFASC; NOPE; NPHS1; NRCAM; OBSCN; OBSL1; OSMR; PHYHIP; PHYHIPL; PRLR; PRODH2; PTPRB; PTPRC; PTPRD; PTPRF; PTPRG; PTPRH; PTPRJ; PTPRK; PTPRM; PTPRO; PTPRS; PTPRT; PTPRU; PTPRZ1; PTPsigma; PUNC; RIMBP2; ROBO1; ROBO2; ROBO3; ROBO4; ROS1; SDK1; SDK2; SNED1; SORL1; SPEG; TEK; TIE1; TNC; TNN; TNR; TNXB; TRIM36; TRIM42; TRIM46; TRIM67; TRIM9; TTN; TYRO3; UMODL1; USH2A; VASN; VWA1; dJ34F7.1; fmi;

See also

  • Monobodies are engineered (synthetic) antibody mimetics based on a fibronectin type III domain (specifically, the 10th FN3 domain of human fibronectin). Monobodies feature either diversified loops or diversified strands of a flat beta-sheet surface, which serve as interaction epitopes. Monobody binders have been selected a wide variety of target molecules, and have expanded beyond the potential range of binding interfaces observed in both natural and synthetic antibodies.

References

  • Bazan JF (September 1990). "Structural design and molecular evolution of a cytokine receptor superfamily". Proceedings of the National Academy of Sciences of the United States of America. 87 (18): 6934–8. doi:10.1073/pnas.87.18.6934. PMC 54656. PMID 2169613.
  • Little E, Bork P, Doolittle RF (December 1994). "Tracing the spread of fibronectin type III domains in bacterial glycohydrolases". Journal of Molecular Evolution. 39 (6): 631–43. doi:10.1007/bf00160409. PMID 7528812.
  • Kornblihtt AR, Umezawa K, Vibe-Pedersen K, Baralle FE (July 1985). "Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene". The EMBO Journal. 4 (7): 1755–9. PMC 554414. PMID 2992939.