4.0 Article

NMR resonance assignment of a fibroblast growth factor 8 splicing isoform b

Journal

BIOMOLECULAR NMR ASSIGNMENTS
Volume 17, Issue 1, Pages 135-142

Publisher

SPRINGER
DOI: 10.1007/s12104-023-10132-8

Keywords

Fibroblast growth factor; FGF8b; FGF8; FGF; Structure; Dynamics; Motions; FGFR; Fibroblast growth factor receptor

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We report the NMR chemical shift assignment of FGF8b, an important regulator of brain embryonic development in humans. The obtained chemical shifts agree with X-ray data, except for the N-terminal gN helix which forms only when complexed with the receptor. This data serves as a starting point for investigating the interaction of FGF8b with its receptors and potential drugs or inhibitors.
The splicing isoform b of human fibroblast growth factor 8 (FGF8b) is an important regulator of brain embryonic development. Here, we report the almost complete NMR chemical shift assignment of the backbone and aliphatic side chains of FGF8b. Obtained chemical shifts are in good agreement with the previously reported X-ray data, excluding the N-terminal gN helix, which apparently forms only in complex with the receptor. The reported data provide an NMR starting point for the investigation of FGF8b interaction with its receptors and with potential drugs or inhibitors.

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