Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions.

The protein tyrosine kinase c-Src is negatively regulated by phosphorylation of Tyr527 in its C-terminal tail. The repressed state is achieved through intramolecular interactions involving the phosphorylated tail, the Src homology 2 (SH2) domain and the SH3 domain. Both the SH2 and SH3 domains have...

Täydet tiedot

Bibliografiset tiedot

Julkaisussa:	EMBO J
Päätekijät:	Erpel, T, Superti-Furga, G, Courtneidge, S A
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	Nature Publishing Group 1995
Aiheet:	Research Article
Linkit:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC398168/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7534229/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1995.tb07077.x
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