Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3-OH kinase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-08

AUTHORS

G W Booker, A L Breeze, A K Downing, G Panayotou, I Gout, M D Waterfield, I D Campbell

ABSTRACT

Receptor protein-tyrosine kinases, through phosphorylation of specific tyrosine residues, generate high-affinity binding sites which direct assembly of multienzyme signalling complexes. Many of these signalling proteins, including phospholipase C gamma, GTPase-activating protein and phosphatidylinositol-3-OH kinase, contain src-homology 2 (SH2) domains, which bind with high affinity and specificity to tyrosine-phosphorylated sequences. The critical role played by SH2 domains in signalling has been highlighted by recent studies showing that mutation of specific phosphorylation sites on the platelet-derived growth factor receptor impair its association with phosphatidylinositol-3-OH kinase, preventing growth factor-induced mitogenesis. Here we report the solution structure of an isolated SH2 domain from the 85K regulatory subunit of phosphatidylinositol-3-OH kinase, determined using multidimensional nuclear magnetic resonance spectroscopy. The structure is characterized by a central region of beta-sheet flanked by two alpha-helices, with a highly flexible loop close to functionally important residues previously identified by site-directed mutagenesis. More... »

PAGES

684-687

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/358684a0

DOI

http://dx.doi.org/10.1038/358684a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045636554

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1323062


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