Crystal structure of a complex between protein tyrosine phosphatase 1B and the insulin receptor tyrosine kinase (Q24293674)

4

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author name string

Shiqing Li

1

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Rafael S Depetris

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David Barford

Shape complementarity at protein/protein interfaces

3

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language of work or name

English

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publication date

November 2005

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published in

Structure

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volume

13

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issue

11

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page(s)

1643-51

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cites work

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APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase

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Interaction of protein tyrosine phosphatase (PTP) 1B with its substrates is influenced by two distinct binding domains

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SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase

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Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)

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Protein-tyrosine phosphatase 1B complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulin

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Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B.

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