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

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

Research output: Contribution to journalArticle

543 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)646-653
Number of pages8
JournalNature
Volume358
Issue number6388
StatePublished - Aug 20 1992
Externally publishedYes

Fingerprint

Phosphotyrosine
src Homology Domains
Tyrosine
src Genes
Peptides
Oncogene Proteins
X Ray Crystallography
Hydrogen Bonding
Lysine
Arginine
Phosphates

ASJC Scopus subject areas

  • General

Cite this

Waksman, G., Kominos, D., Robertson, S. C., Pant, N., Baltimore, D., Birge, R. B., ... Kuriyan, J. (1992). Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature, 358(6388), 646-653.

Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. / Waksman, Gabriel; Kominos, Dorothea; Robertson, Scott C.; Pant, Nalin; Baltimore, David; Birge, Raymond B.; Cowburn, David; Hanafusa, Hidesaburo; Mayer, Bruce J.; Overduin, Michael; Resh, Marilyn D.; Rios, Carlos B.; Silverman, Lauren; Kuriyan, John.

In: Nature, Vol. 358, No. 6388, 20.08.1992, p. 646-653.

Research output: Contribution to journalArticle

Waksman, G, Kominos, D, Robertson, SC, Pant, N, Baltimore, D, Birge, RB, Cowburn, D, Hanafusa, H, Mayer, BJ, Overduin, M, Resh, MD, Rios, CB, Silverman, L & Kuriyan, J 1992, 'Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides', Nature, vol. 358, no. 6388, pp. 646-653.
Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, Birge RB et al. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature. 1992 Aug 20;358(6388):646-653.
Waksman, Gabriel ; Kominos, Dorothea ; Robertson, Scott C. ; Pant, Nalin ; Baltimore, David ; Birge, Raymond B. ; Cowburn, David ; Hanafusa, Hidesaburo ; Mayer, Bruce J. ; Overduin, Michael ; Resh, Marilyn D. ; Rios, Carlos B. ; Silverman, Lauren ; Kuriyan, John. / Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. In: Nature. 1992 ; Vol. 358, No. 6388. pp. 646-653.
@article{165bee14d53b4b308143fb3e73d4607a,
title = "Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides",
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 {\AA}, 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.",
author = "Gabriel Waksman and Dorothea Kominos and Robertson, {Scott C.} and Nalin Pant and David Baltimore and Birge, {Raymond B.} and David Cowburn and Hidesaburo Hanafusa and Mayer, {Bruce J.} and Michael Overduin and Resh, {Marilyn D.} and Rios, {Carlos B.} and Lauren Silverman and John Kuriyan",
year = "1992",
month = "8",
day = "20",
language = "English (US)",
volume = "358",
pages = "646--653",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6388",

}

TY - JOUR

T1 - Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

AU - Waksman, Gabriel

AU - Kominos, Dorothea

AU - Robertson, Scott C.

AU - Pant, Nalin

AU - Baltimore, David

AU - Birge, Raymond B.

AU - Cowburn, David

AU - Hanafusa, Hidesaburo

AU - Mayer, Bruce J.

AU - Overduin, Michael

AU - Resh, Marilyn D.

AU - Rios, Carlos B.

AU - Silverman, Lauren

AU - Kuriyan, John

PY - 1992/8/20

Y1 - 1992/8/20

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0026698924&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026698924&partnerID=8YFLogxK

M3 - Article

C2 - 1379696

AN - SCOPUS:0026698924

VL - 358

SP - 646

EP - 653

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6388

ER -