@article{964f42949c2c4c4b96f75fcfaf375de2,
title = "Three-dimensional solution structure of the src homology 2 domain of c-abl",
abstract = "SH2 regions are protein motifs capable of binding target protein sequences that contain a phosphotyrosine. The solution structure of the abl SH2 product, a protein of 109 residues and 12.1 kd, has been determined by multidimensional nuclear magnetic resonance spectroscopy. It is a compact spherical domain with a pair of three-stranded antiparallel β sheets and a C-terminal α helix enclosing the hydrophobic core. Three arginines project from a short N-terminal α helix and one β sheet into the putative phosphotyrosine-binding site, which lies on a face distal from the termini. Comparison with other SH2 sequences supports a common global fold and mode of phosphotyrosine binding for this family.",
author = "Michael Overduin and Rios, {Carlos B.} and Mayer, {Bruce J.} and David Baltimore and David Cowburn",
note = "Funding Information: This work was supported by grants (CA-51462 to D. B.; DK-20357 and GM-47021 to D. C.) and fellowships (CA-0887501 to B. J. M. and GM-14313 to C. B. R.) from the National Institutes of Health, and an unrestricted gift from American Cynamid (D. C.). NMR resources were purchased with grants from NIH, the Keck Foundation, and the National Science Foundation. 8. J. M. and D. B gratefully acknowledge the contribution of Peter Jackson, who initiated experiments leading to this work. Drs. P. Giintert and K. Wiithrich provided the DIANA program and useful advice. Biosym Technologies, Inc., provided helpful cooperation. We are grateful to Professor John Kuriyan for his advice and comments on molecular displays and to him and Professor Stephen Burley for the use of computer graphics facilities, and to Drs. Marius Clore, Nalin Pant, and Yuying Gosser for discussion. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.",
year = "1992",
month = aug,
day = "21",
doi = "10.1016/0092-8674(92)90437-H",
language = "English (US)",
volume = "70",
pages = "697--704",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "4",
}