Structure and ligand recognition of the phosphotyrosine binding domain of Shc View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-12

AUTHORS

M M Zhou, K S Ravichandran, E F Olejniczak, A M Petros, R P Meadows, M Sattler, J E Harlan, W S Wade, S J Burakoff, S W Fesik

ABSTRACT

The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of Shc complexed to a phosphopeptide reveals an alternative means of recognizing tyrosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel beta-strand with a beta-sheet of the protein, interacts with a hydrophobic pocket through the (pY-5) residue, and adopts a beta-turn. The PTB domain is structurally similar to pleckstrin homology domains (a beta-sandwich capped by an alpha-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization. More... »

PAGES

584-592

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/378584a0

DOI

http://dx.doi.org/10.1038/378584a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029778580

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8524391


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