Literature DB >> 8524391

Structure and ligand recognition of the phosphotyrosine binding domain of Shc.

M M Zhou1, 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.

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Year:  1995        PMID： 8524391     DOI： 10.1038/378584a0

Source DB:  PubMed          Journal:  Nature        ISSN： 0028-0836            Impact factor:   49.962


  92 in total

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Review 5.  Protein-protein interactions in signaling cascades.

Authors:  B J Mayer
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6.  Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo.

Authors:  K S Ravichandran; M M Zhou; J C Pratt; J E Harlan; S F Walk; S W Fesik; S J Burakoff
Journal:  Mol Cell Biol       Date:  1997-09       Impact factor: 4.272

7.  The role of the PH domain in the signal-dependent membrane targeting of Sos.

Authors:  R H Chen; S Corbalan-Garcia; D Bar-Sagi
Journal:  EMBO J       Date:  1997-03-17       Impact factor: 11.598

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Authors:  K H Gardner; R Konrat; M K Rosen; L E Kay
Journal:  J Biomol NMR       Date:  1996-10       Impact factor: 2.835

10.  p66Shc Couples Mechanical Signals to RhoA through Focal Adhesion Kinase-Dependent Recruitment of p115-RhoGEF and GEF-H1.

Authors:  Ru-Feng Wu; Chengxu Liao; Guosheng Fu; Heather N Hayenga; Kejia Yang; Zhenyi Ma; Zhe Liu; Lance S Terada
Journal:  Mol Cell Biol       Date:  2016-10-28       Impact factor: 4.272
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