Author:
Hargittay Bruno,Mineev Konstantin S.,Richter Christian,Sreeramulu Sridhar,Jonker Hendrik R.A.,Saxena Krishna,Schwalbe Harald
Abstract
AbstractThe 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.
Funder
Johann Wolfgang Goethe-Universität, Frankfurt am Main
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Cited by
1 articles.
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