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Diversity in protein recognition by PTB domains

Forman-Kay, Julie D, Pawson, Tony·1999·Current Opinion in Structural Biology
DOI 10.1016/s0959-440x(99)00031-7
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Abstract

Phosphotyrosine-binding (PTB) domains were originally identified as modular domains that recognize phosphorylated Asn-Pro-Xxx-p Tyr-containing proteins. Recent binding and structural studies of PTB domain complexes with target peptides have revealed a number of deviations from the previously described mode of interaction, with respect to both the sequences of possible targets and their structures within the complexes. This diversity of recognition by PTB domains extends and strengthens our general understanding of modular binding domain recognition.

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  • PTB domains of adaptor proteins such as SHC, IRS-1, X11, Dab-1, and Dab-2 bind a canonical NPXY sequence motif in cytoplasmic tails of various cell surface receptors.

    “The PTB domains of adaptor proteins such as SHC, IRS-1, X11, Dab-1, and Dab-2 bind a canonical sequence motif (NPXY) in the cytoplasmic tails of various cell surface receptors (8”

    From ARH Is a Modular Adaptor Protein That Interacts with the LDL Receptor, Clathrin, and AP-2 (2002) · cites this paper as [8]

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Metadata

Authors
Forman-Kay, J. D., & Pawson, T.
Venue
Current Opinion in Structural Biology
Publisher
Elsevier BV
Published
1999-12
Volume
9
Issue
6
Pages
690-695
ISSN
0959-440X
DOI
10.1016/s0959-440x(99)00031-7
Cited by
98
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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