Methods used in the Assignments of the 1H and 15N resonances of the c-Abl src homology 2 (SH2) domain View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1994

AUTHORS

Michael Overduin , Carlos B. Rios , Bruce J. Mayer , David Baltimore , David Cowburn

ABSTRACT

The SH2 domain is a recognition motif of approximately 100 amino acids that serves to mediate the association of cytoplasmic proteins involved in signal transduction. SH2 domains from a number of proteins, including Crk, phospholipase C-γ, Ras GTPase-activating protein and Abl, have been shown to bind specifically protein sequences that have been phosphorylated on tyrosine residues (Anderson et al1990; Margolis et al, 1990; Mayer and Hanafusa et al, 1990; Mayer et al, 1991; Moran et al, 1990). The transforming activity of Abl depends on the highly conserved FLVRESES motif, a central element in the binding of tyrosine phosphorylated ligands (Mayer et al, 1992). More... »

PAGES

189-198

Book

TITLE

NMR of Biological Macromolecules

ISBN

978-3-642-79160-4
978-3-642-79158-1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-642-79158-1_9

DOI

http://dx.doi.org/10.1007/978-3-642-79158-1_9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1039073289


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