Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-08

AUTHORS

Gabriel Waksman, Dorothea Kominos, Scott C. Robertson, Nalin Pant, David Baltimore, Raymond B. Birge, David Cowburn, Hidesaburo Hanafusa, Bruce J. Mayer, Michael Overduin, Marilyn D. Resh, Carlos B. Rios, Lauren Silverman, John Kuriyan

ABSTRACT

Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 Å, respectively. A central antiparallel β-sheet in the structure is flanked by two α-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino–aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate. More... »

PAGES

646-653

Journal

TITLE

Nature

ISSUE

6388

VOLUME

358

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/358646a0

DOI

http://dx.doi.org/10.1038/358646a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021461565

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1379696


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