Structure and ligand recognition of the phosphotyrosine binding domain of Shc

Ming Ming Zhou; Kodimangalam S. Ravichandran; Edward T. Olejniczak; Andrew M. Petros; Robert P. Meadows; Michael Sattler; John E. Harlan; Warren S. Wade; Steven J. Burakoff; Stephen W. Fesik

doi:10.1038/378584a0

Structure and ligand recognition of the phosphotyrosine binding domain of Shc

Ming Ming Zhou, Kodimangalam S. Ravichandran, Edward T. Olejniczak, Andrew M. Petros, Robert P. Meadows, Michael Sattler, John E. Harlan, Warren S. Wade, Steven J. Burakoff, Stephen W. Fesik

Research output: Contribution to journal › Article › peer-review

327 Scopus citations

Abstract

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

Original language	English
Pages (from-to)	584-592
Number of pages	9
Journal	Nature
Volume	378
Issue number	6557
DOIs	https://doi.org/10.1038/378584a0
State	Published - 7 Dec 1995
Externally published	Yes

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@article{70a1370afd57469f9372307e0fbff33a,

title = "Structure and ligand recognition of the phosphotyrosine binding domain of Shc",

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

author = "Zhou, {Ming Ming} and Ravichandran, {Kodimangalam S.} and Olejniczak, {Edward T.} and Petros, {Andrew M.} and Meadows, {Robert P.} and Michael Sattler and Harlan, {John E.} and Wade, {Warren S.} and Burakoff, {Steven J.} and Fesik, {Stephen W.}",

year = "1995",

month = dec,

day = "7",

doi = "10.1038/378584a0",

language = "English",

volume = "378",

pages = "584--592",

journal = "Nature",

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TY - JOUR

T1 - Structure and ligand recognition of the phosphotyrosine binding domain of Shc

AU - Zhou, Ming Ming

AU - Ravichandran, Kodimangalam S.

AU - Olejniczak, Edward T.

AU - Petros, Andrew M.

AU - Meadows, Robert P.

AU - Sattler, Michael

AU - Harlan, John E.

AU - Wade, Warren S.

AU - Burakoff, Steven J.

AU - Fesik, Stephen W.

PY - 1995/12/7

Y1 - 1995/12/7

N2 - The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of She complexed to a phosphopeptide reveals an alternative means of recognizing tryosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel β-strand with a β-sheet of the protein, interacts with a hydrophobic pocket through the (pY–5) residue, and adopts a β-turn. The PTB domain is structurally similar to pleckstrin homology domains (a β-sandwich capped by an α-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization.

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

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U2 - 10.1038/378584a0

DO - 10.1038/378584a0

M3 - Article

C2 - 8524391

AN - SCOPUS:0028860968

SN - 0028-0836

VL - 378

SP - 584

EP - 592

JO - Nature

JF - Nature

IS - 6557

ER -

Structure and ligand recognition of the phosphotyrosine binding domain of Shc

Abstract

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