BAIT

NCAM1

Cd56, N-CAM, N-CAM-1, NCAM-1, NCAM-C, NCAMC, Ncam
neural cell adhesion molecule 1
Rattus norvegicus
PREY

FGFR1

AW208770, Eask, FLG, Fgfr-1, Flt-2, Hspy, MFR, bFGF-R-1, c-fgr
fibroblast growth factor receptor 1
GO Process (41)
GO Function (3)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Mus musculus

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Structural basis for a direct interaction between FGFR1 and NCAM and evidence for a regulatory role of ATP.

Kiselyov VV, Skladchikova G, Hinsby AM, Jensen PH, Kulahin N, Soroka V, Pedersen N, Tsetlin V, Poulsen FM, Berezin V, Bock E

The neural cell adhesion molecule (NCAM) promotes axonal outgrowth, presumably through an interaction with the fibroblast growth factor receptor (FGFR). NCAM also has a little-understood ATPase activity. We here demonstrate for the first time a direct interaction between NCAM (fibronectin type III [F3] modules 1 and 2) and FGFR1 (Ig modules 2 and 3) by surface plasmon resonance (SPR) analysis. ... [more]

Structure Jun. 01, 2003; 11(6);691-701 [Pubmed: 12791257]

Throughput

  • Low Throughput

Additional Notes

  • Surface plasmon resonance

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
NCAM1 FGFR1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
2469319

Curated By

  • BioGRID