Structural insights into the intertwined dimer of Fyn SH2

Radu Ion Huculeci, Abel Garcia Pino, Lieven Buts, Tom Lenaerts, Nico Van Nuland

Onderzoeksoutput: Articlepeer review

7 Citaten (Scopus)

Samenvatting

Src homology 2 domains are interaction modules dedicated to the recognition of phosphotyrosine sites incorporated in numerous proteins found in intracellular signaling pathways. Here we provide for the first time structural insight into the dimerization of Fyn SH2 both in solution and in crystalline conditions, providing novel crystal structures of both the dimer and peptide-bound structures of Fyn SH2. Using nuclear magnetic resonance chemical shift analysis, we show how the peptide is able to eradicate the dimerization, leading to monomeric SH2 in its bound state. Furthermore, we show that Fyn SH2's dimer form differs from other SH2 dimers reported earlier. Interestingly, the Fyn dimer can be used to construct a completed dimer model of Fyn without any steric clashes. Together these results extend our understanding of SH2 dimerization, giving structural details, on one hand, and suggesting a possible physiological relevance of such behavior, on the other hand.
Originele taal-2English
Pagina's (van-tot)1964-1978
Aantal pagina's15
TijdschriftProtein Science
Volume24
Nummer van het tijdschrift12
Vroegere onlinedatum7 okt 2015
DOI's
StatusPublished - dec 2015

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